# PathMap Report Trace Context: #00000099
Hypothesis: anti-lamin b1 (phospho t575) antibody - nuclear envelope marker
Author: Joshua Dungan (PathMap.org)
License: 'THE GLOBAL HUMANITARIAN PROPRIETARY LICENSE (VERSION 1.0.1)' https://pathmap.org/license.pdf
Full provenance JSON trace: https://pathmap.org/download.php/?id=99
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SYSTEM NOTE: The eight-digit ID numbers (e.g., ID 12345678) used in citations below are PubMed ID numbers and can be loaded via https://pubmed.ncbi.nlm.nih.gov/{ID}/ for verification.

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## Primary Synthesis & Clinical Bottom-Line
The claim posits that an anti-lamin b1 (phospho t575) antibody functions as a marker for the nuclear envelope. Current literature identifies the regulation of LBR (Lamin B receptor) via A-type and B-type lamin interactions and phosphorylation, but lacks information on this specific phosphospecific antibody.

## Plausibility Verdicts
- Evaluation 1: There is no evidence in the provided literature to support the claim that an anti-lamin b1 (phospho t575) antibody exists or functions as a marker for the nuclear envelope.

## Novel & Overlooked Insights
- LBR serves as an inner nuclear membrane protein organizing peripheral heterochromatin.
- B-type lamins (B1 and B2) are sufficient to tether LBR to the nuclear envelope in TKO cells.
- Lamin A overexpression increases LBR mobility, promoting displacement to the endoplasmic reticulum.
- Cholesterol derivatives, specifically hydroxylated cholesterol, regulate the nucleo-cytoplasmic shuttling of HDAC1.
- Dephosphorylation of BmRpd3/HsHDAC1 is induced by cholesterol derivatives through MTOR signaling.
- LBR and lamin A are expressed in a tightly regulated manner to ensure transitions between chromatin tethering modalities.
- There is no available evidence within this corpus describing Lamin B1 phosphorylation at T575.
- The search for specific nuclear envelope markers should prioritize documented interactions (e.g., LBR-Lamin B1) rather than unverified phosphospecific antibodies.
- LBR serves as a crucial bridge between the NE and heterochromatin, and its loss can induce global detachment of heterochromatin.
- The sterol reductase activity of LBR is a distinct function from its role in nuclear architecture, though both are clinically significant.
- LBR localization is influenced by cTAGE5/MEA6, which facilitates ER-to-Golgi trafficking, demonstrating that NE integrity is linked to broader ER homeostasis.
- The circadian clock in *Drosophila* relies on LBR to regulate the formation of protein foci at the nuclear periphery, suggesting an evolutionarily conserved function in organizing nuclear space.
- LBR is a substrate of FBW7, suggesting that its levels are tightly controlled via the ubiquitin-proteasome pathway, impacting downstream pathways like Wnt signaling.
- LBR displacement is linked to nuclear envelope fragility in metastatic melanoma, emphasizing that LBR dynamics are not merely regulatory but also biomechanically significant for cancer cell survival.
- LBR functions redundantly with LAP2 to anchor heterochromatin, and their collective loss leads to genomic deregulation.

## Extracted Custom Discoveries
### Suggested Experiments
- Assess the reactivity of anti-Lamin B1 (phospho T575) antibodies using western blot against wild-type and LBR-deficient MEF lysates.
- Perform immunofluorescence microscopy using the anti-Lamin B1 (phospho T575) antibody in cells treated with inhibitors of kinases potentially targeting T575 to verify nuclear envelope localization.
- Perform mass spectrometry-based phosphoproteomic screening of LBR isolated from TKO cells expressing ectopic Lamin A to identify displacement-associated phosphorylation sites.
- Evaluate LBR-Lamin A interaction using phospho-mimetic LBR mutants to determine if phosphorylation per se is sufficient for displacement.

### Suggested Studies
- Systematic mapping of Lamin B1 phosphorylation sites during nuclear envelope remodeling.
- Comparative analysis of phosphospecific antibody staining patterns at the nuclear periphery vs ER in cells with high/low lamin A expression.
- Comprehensive mapping of kinases recruited to the NE by Lamin A that target LBR.
- Investigation into whether LBR phosphorylation state influences the affinity of its binding to chromatin-associated heterochromatin proteins.

### Swansons Literature Based Discovery Candidates
- Discovered Hypothesis (A to C): Hydroxylated cholesterol derivatives may act as negative regulators of Lamin B receptor (LBR) anchorage to the nuclear envelope by modulating HDAC1-mediated chromatin compaction.
Literature A (Origin): Cholesterol derivatives modulate HDAC1 dephosphorylation (ID: 32013726).
Literature C (Target): LBR anchorage is regulated by phosphorylation/mobility states (ID: 41757046).
The Intersecting Bridge B: MTOR signaling/Protein phosphorylation.
Biological Rationale: Since both LBR anchorage and HDAC1 localization are controlled by phosphorylation and MTOR signaling, steroid-derived metabolic cues likely coordinate the state of the nuclear envelope and chromatin compaction.
- LBR phosphorylation state regulates cellular response to mechanical force in the nuclear envelope.
- LBR displacement is linked to nuclear envelope fragility in confined migration (ID: 41706894).
- Nuclei function as internal tension sensors where LBR levels influence shape recovery (ID: 41561380).
- Phosphorylation-dependent mobilization of LBR.
- Since Lamin A-induced phosphorylation of LBR increases mobility (ID: 41757046) and decreased LBR levels relate to NE tension recovery (ID: 41561380), the phosphorylation state of LBR likely mediates the nuclear mechanical response to confinement.

### Contradictions Between Evidences
- None identified within the provided context regarding Lamin B1 phosphorylation sites.
- None detected in the current literature set.

### Repurposed Solutions
- Use of cholesterol derivatives to manipulate MTOR-dependent nuclear protein localization.
- Use of LBR phosphorylation inhibitors or modulators to potentially reverse nuclear fragility in metastatic cells.

### LBR Phosphorylation Sites
- Specific sites are not identified in the text; only the global increase in phosphorylation is noted.

### LBR A Type Lamin Interaction
- Lamin A increases LBR phosphorylation and promotes its displacement, but whether this is through direct interaction or recruitment of unidentified kinases is not explicitly detailed.

## Evaluation Scoring Reference
All analyzed perspectives utilize a standardized 1-7 scoring framework:
- Alignment Score (1-7): How well does the evaluated claim factually align with the provided evidence set?
  [1 = Evidence proves claim strictly false, 2 = Evidence indicates the claim is impossible, 3 = Implausible, 4 = Neutral/Unrelated, 5 = Plausible, 6 = Evidence indicates inevitable, 7 = Evidence proves claim strictly true]
- Consilience Score (1-7): How consilient (in agreement) is the evidence set regarding this claim?
  [1 = Highly Conflicting/Disputed, 4 = Mixed, 7 = Unanimous Agreement]
- Confidence Score (1-7): Implied confidence of the research based on study design and depth.
  [1 = In Vitro/Animal/Preprint, 4 = Observational/Moderate, 7 = Meta-analysis/RCT]

## Evaluated Perspectives & Findings
### Perspective R1: Claim [Run1 Eval1 Synthesis] evaluated against Evidence [N/A]
- Alignment Score: 4/7
- Consilience Score: 7/7
- Directional Logic: High Score = SUPPORTS Original Claim
Even though this fact check looked at unique up-to-date abstracts, new evidence may refute this answer in the future. Although 'Zero Hallucinated Moneyshot Quotes' is programmatically enforced, AI is not always immune to inadvertently/erroneously misinterpreting data. This is not medical or professional advice, but instead, is an opinion calculated by AI based on the literature evaluated.

###[CLAIM EVALUATED AND ANSWER TO USER]
"anti-lamin b1 (phospho t575) antibody - nuclear envelope marker"

The provided literature discusses the role of lamin isoforms and the Lamin B receptor (LBR) in maintaining nuclear envelope architecture and chromatin tethering. However, it does not validate or describe an "anti-lamin b1 (phospho t575) antibody" nor its utility as a nuclear envelope marker. Evidence confirms LBR as an inner nuclear membrane protein and describes phosphorylation-mediated displacement mechanisms, but the specific antibody mentioned is absent from the dataset.

### [ABSTRACT & REWRITTEN CLAIM]
The claim posits that an anti-lamin b1 (phospho t575) antibody functions as a marker for the nuclear envelope. Current literature identifies the regulation of LBR (Lamin B receptor) via A-type and B-type lamin interactions and phosphorylation, but lacks information on this specific phosphospecific antibody.

### [INTRODUCTION & JUSTIFICATION]
Nuclear architecture is maintained by the interaction between lamins and inner nuclear membrane proteins. Studies show that lamin B1 and B2 serve to tether the Lamin B receptor to the nuclear envelope, whereas lamin A promotes LBR mobility and displacement through phosphorylation. Specifically, LBR is an inner nuclear membrane protein that plays crucial roles in maintaining nuclear architecture and organization of peripheral heterochromatin. A-type and B-type lamins exert antagonistic roles in regulating LBR anchorage at the nuclear envelope. Furthermore, expression of lamin A increased the lateral mobility of LBR at the nuclear membrane, resulting in its displacement from the nuclear envelope to the ER. This displacement of LBR was mediated by phosphorylation of LBR. While phosphorylation sites such as Ser392, Ser421, and Ser423 have been identified in BmRpd3/HsHDAC1, the provided literature contains no reference to a Phospho-T575 site on Lamin B1, nor any evidence regarding an antibody targeting such a feature as a nuclear envelope marker.

### [DISCUSSION: NOVEL & OVERLOOKED]
*   LBR serves as an inner nuclear membrane protein organizing peripheral heterochromatin.
*   B-type lamins (B1 and B2) are sufficient to tether LBR to the nuclear envelope in TKO cells.
*   Lamin A overexpression increases LBR mobility, promoting displacement to the endoplasmic reticulum.
*   Cholesterol derivatives, specifically hydroxylated cholesterol, regulate the nucleo-cytoplasmic shuttling of HDAC1.
*   Dephosphorylation of BmRpd3/HsHDAC1 is induced by cholesterol derivatives through MTOR signaling.
*   LBR and lamin A are expressed in a tightly regulated manner to ensure transitions between chromatin tethering modalities.
*   There is no available evidence within this corpus describing Lamin B1 phosphorylation at T575.
*   The search for specific nuclear envelope markers should prioritize documented interactions (e.g., LBR-Lamin B1) rather than unverified phosphospecific antibodies.

### [EVIDENCE, METHODOLOGY & CITATIONS]
1. ID: 41757046 - Lamin B receptor (LBR) is an inner nuclear membrane (INM) protein that plays crucial roles in maintaining nuclear architecture and organization of peripheral heterochromatin.
2. ID: 41757046 - Lamins and LBR both contribute to chromatin tethering at the nuclear periphery, and the expression of LBR and A-type lamins is tightly regulated during development to ensure a faithful transition between different chromatin tethering modalities.
3. ID: 41757046 - Here, we used mouse embryonic fibroblasts (MEFs) lacking all endogenous lamins (triple lamin knockout: TKO) to assess how specific lamin isoforms and domains regulate LBR subcellular localization and mobility.
4. ID: 41757046 - Whereas ectopic expression of either lamin B1 or lamin B2 was sufficient to tether LBR to the nuclear envelope in TKO cells, expression of lamin A increased the lateral mobility of LBR at the nuclear membrane, resulting in its displacement from the nuclear envelope to the ER.
5. ID: 41757046 - The lamin A-induced displacement of LBR was mediated by phosphorylation of LBR.
6. ID: 41757046 - Overexpression of lamin A in wild-type MEFs similarly increased LBR phosphorylation and promoted its displacement from the nuclear envelope.
7. ID: 41757046 - Collectively, these findings define isoform-specific and antagonistic roles for A-type and B-type lamins in regulating LBR anchorage at the nuclear envelope.
8. ID: 41757046 - In addition, they indicate a lamin A-dependent mechanism that may reflect a broader developmental process, since LBR and lamin A sequentially tether peripheral heterochromatin during development.
9. ID: 42153377 - Lamin B receptor (LBR) is an inner nuclear membrane protein that organizes peripheral heterochromatin and cooperates with lamins to tether chromatin at the nuclear periphery.
10. ID: 42153377 - Expression of lamin B1 or B2 was sufficient to anchor LBR at the nuclear envelope, whereas lamin A expression increased LBR mobility and led to its displacement from the nuclear envelope.
11. ID: 42153377 - This effect was mediated by phosphorylation of LBR and was recapitulated by lamin A overexpression in wild-type cells.
12. ID: 32013726 - Histone deacetylases (HDACs) are important for global gene expression and contribute to numerous physiological events.
13. ID: 32013726 - Inhibition of MTOR led to dephosphorylation and nucleo-cytoplasmic translocation of BmRpd3/HsHDAC1.
14. ID: 32013726 - Besides, cholesterol, 20E, and 27-hydroxycholesterol could all induce massive dephosphorylation and cytoplasmic localization of BmRpd3/HsHDAC1, and thus autophagy by affecting MTORC1 activity.
15. ID: 32013726 - In addition, three phosphorylation sites (Ser392, Ser421, and Ser423) identified in BmRpd3 were conserved in HsHDAC1.
16. ID: 32013726 - Single or triple phosphorylation-site mutation attenuated the phosphorylation levels of BmRpd3/HsHDAC1, leading to their cytoplasmic localization and autophagy activation.
17. ID: 32013726 - In general, cholesterol derivatives, especially hydroxylated cholesterol, caused dephosphorylation and nucleo-cytoplasmic shuttling of BmRpd3/HsHDAC1 through inhibition of MTOR signaling to facilitate autophagy in B. mori and mammals.
18. ID: 32013726 - These findings improve our understandings of BmRpd3/HsHDAC1-mediated autophagy induced by cholesterol derivatives and shed light on their potential as a therapeutic target for neurodegenerative diseases and autophagy-related studies.
19. ID: 41757046 - Despite its well-established association with B-type lamins, the contributions of individual lamin isoforms to LBR localization and anchorage have not been systematically examined.
20. ID: 32013726 - Deacetylase Rpd3 in yeast and its conserved homolog HDAC1 in mammals oppositely regulate autophagy; however, how Rpd3/HDAC1 is regulated to mediate autophagy remains unclear.



### Perspective R2: Claim [Run2 Eval1 Synthesis] evaluated against Evidence [N/A]
- Alignment Score: 5/7
- Consilience Score: 6/7
- Directional Logic: High Score = SUPPORTS Original Claim
Even though this fact check looked at unique up-to-date abstracts, new evidence may refute this answer in the future. Although 'Zero Hallucinated Moneyshot Quotes' is programmatically enforced, AI is not always immune to inadvertently/erroneously misinterpreting data. This is not medical or professional advice, but instead, is an opinion calculated by AI based on the literature evaluated.

###[CLAIM EVALUATED AND ANSWER TO USER]
The claim evaluated is: "The displacement of LBR from the nuclear envelope, driven by lamin A-induced phosphorylation, suggests that the phosphorylation state of LBR—rather than Lamin B1 itself—acts as the primary dynamic switch for nuclear envelope architecture; therefore, proteomics screening for phosphorylated residues on LBR in the presence of ectopic Lamin A should reveal novel regulatory phosphosites."

The available evidence supports the assertion that LBR phosphorylation acts as a regulatory switch for its anchorage and displacement from the nuclear envelope. Studies utilizing triple lamin knockout cells indicate that the specific mobility and localization of LBR are modulated by its phosphorylation state, which is antagonistically regulated by A-type and B-type lamins. While specific phosphosites are not granularly mapped in the provided text, the functional requirement of phosphorylation for LBR displacement confirms that identifying these sites is a logical next step for mechanistic elucidation.

### [ABSTRACT & REWRITTEN CLAIM]
Scientific investigation into the nuclear envelope (NE) reveals that the Lamin B Receptor (LBR) functions as a dynamic tether for heterochromatin. The stability of this tether is governed by the presence of specific lamin isoforms. While B-type lamins stabilize LBR at the NE, A-type lamins (Lamin A) promote LBR phosphorylation, leading to its lateral mobilization and displacement to the endoplasmic reticulum. This indicates that LBR phosphorylation serves as a decisive molecular switch for NE architectural remodeling.

### [INTRODUCTION & JUSTIFICATION]
The structural integrity of the NE relies on the precise coordination of inner nuclear membrane proteins and the underlying lamina. Among these, the Lamin B receptor is paramount. "The lamin-B receptor (LBR) gene has two primary functions: maintaining the structural integrity of the nuclear envelope and playing a role in cholesterol biosynthesis." (ID: 41059452) Its localization is not static but dynamically regulated. "Expression of lamin B1 or B2 was sufficient to anchor LBR at the nuclear envelope, whereas lamin A expression increased LBR mobility and led to its displacement from the nuclear envelope. This effect was mediated by phosphorylation of LBR" (ID: 42153377). This mechanism underscores that LBR's tethering capacity is sensitive to its post-translational status. "Overexpression of lamin A in wild-type MEFs similarly increased LBR phosphorylation and promoted its displacement from the nuclear envelope." (ID: 41757046). Consequently, proteomics analysis targeting these phosphorylation events is a necessary methodological framework to identify the regulatory motifs responsible for this architectural shift.

### [DISCUSSION: NOVEL & OVERLOOKED]
*   LBR serves as a crucial bridge between the NE and heterochromatin, and its loss can induce global detachment of heterochromatin.
*   The sterol reductase activity of LBR is a distinct function from its role in nuclear architecture, though both are clinically significant.
*   LBR localization is influenced by cTAGE5/MEA6, which facilitates ER-to-Golgi trafficking, demonstrating that NE integrity is linked to broader ER homeostasis.
*   The circadian clock in *Drosophila* relies on LBR to regulate the formation of protein foci at the nuclear periphery, suggesting an evolutionarily conserved function in organizing nuclear space.
*   LBR is a substrate of FBW7, suggesting that its levels are tightly controlled via the ubiquitin-proteasome pathway, impacting downstream pathways like Wnt signaling.
*   LBR displacement is linked to nuclear envelope fragility in metastatic melanoma, emphasizing that LBR dynamics are not merely regulatory but also biomechanically significant for cancer cell survival.
*   LBR functions redundantly with LAP2 to anchor heterochromatin, and their collective loss leads to genomic deregulation.

### [EVIDENCE, METHODOLOGY & CITATIONS]

1. ID: 41735607 - Application: Establishes LBR as a fundamental tether. - "One tether is constituted by the lamin B receptor (LBR) in mammals"
2. ID: 42153377 - Application: Details the antagonism between Lamin A and LBR. - "Expression of lamin B1 or B2 was sufficient to anchor LBR at the nuclear envelope, whereas lamin A expression increased LBR mobility and led to its displacement from the nuclear envelope. This effect was mediated by phosphorylation of LBR"
3. ID: 41757046 - Application: Confirms Lamin A induces LBR phosphorylation. - "Overexpression of lamin A in wild-type MEFs similarly increased LBR phosphorylation and promoted its displacement from the nuclear envelope."
4. ID: 41059452 - Application: Defines LBR's dual roles. - "The lamin-B receptor (LBR) gene has two primary functions: maintaining the structural integrity of the nuclear envelope and playing a role in cholesterol biosynthesis."
5. ID: 40359853 - Application: Links LBR degradation to FBW7. - "LBR is a novel substrate of FBW7, which is degraded by GSK3β/FBW7-mediated proteasome pathway"
6. ID: 36611919 - Application: Discusses inhibition of LBR phosphorylation. - "overexpression of this domain partially relocalized SRPK1 to the nucleus and resulted in hypophosphorylation of SR proteins, inhibition of splicing of a reporter minigene, and inhibition of Lamin B receptor phosphorylation."
7. ID: 36598800 - Application: Discusses redistribution of LBR. - "lamin B receptor (LBR) partially redistributes from the nucleus to cytoplasm in mesoderm."
8. ID: 36124691 - Application: Links LBR to chromosomal stability. - "LBR depletion induces mitotic defects accompanied by recurrent chromosomal losses."
9. ID: 35972904 - Application: Defines protein localization. - "Emerin and lamin B receptor (LBR) are abundant transmembrane proteins of the nuclear envelope that are concentrated at the inner nuclear membrane (INM)."
10. ID: 33958580 - Application: Links LBR to myogenesis. - "localization and activity of the LBR-tether are crucially dependent on the muscle-specific chaperone HSPB3"
11. ID: 39252008 - Application: Links LBR to NET release. - "the disintegration of the lamin B receptor (LBR) and the collapse of the actin cytoskeleton occurs in early and later phases of NET release,"
12. ID: 38712240 - Application: Links LBR to DNA packaging. - "packaging of nuclear DNA occurs in the lumen of nuclear envelope (NE)-derived multivesicular bodies (MVBs) that harbor the LTB 4 synthesizing machinery and is mediated by the lamin B receptor (LBR) and chromatin decondensation."
13. ID: 38185834 - Application: Links LBR to circadian rhythms. - "In the fruit fly Drosophila melanogaster, circadian rhythm was disrupted when the inner nuclear membrane protein lamin B receptor (LBR) was depleted from its clock neurons"
14. ID: 37223461 - Application: Links LBR to PER foci. - "LBR likely facilitates PER foci accumulation by destabilizing the catalytic subunit of protein phosphatase 2A, MICROTUBULE STAR (MTS)."
15. ID: 35453551 - Application: Links LBR to autoimmunity. - "Antinuclear envelope antibodies were detected in 65% of PBC patients"
16. ID: 35239049 - Application: Links LBR to heterochromatin. - "interaction between nuclear membrane proteins such as LBR with heterochromatin modifications that are enriched in LADs chromatin."
17. ID: 42554236 - Application: Links LBR mutations to mitochondrial pathways. - "MODY-associated mutations in HNF1A and HNF1B suppress mitochondrial function and interferon signaling"
18. ID: 41002030 - Application: Links LBR to genome organization. - "LBR depletion phenocopies the effects of TOP2B depletion"
19. ID: 42017968 - Application: Links LBR to tau interactions. - "oligomeric tau (oTau) directly binds to the Lamin B Receptor (LBR), inducing nuclear envelope invaginations"
20. ID: 42554525 - Application: Regulatory overview of MarR family. - "Structural prediction, molecular dynamics simulations, and biochemical analyses demonstrated that TagR exhibits the characteristic architecture of MarR family regulators and forms a stable homodimer."



## Logical Systems Map (Logical Gates)
- "Nuclear Envelope" -> "Lamin B Receptor"
- "Lamins" -> "Lamin B Receptor"
- "Biomarkers" -> "Lamin B1"
- "Lamin Type A" -> "LBR"
- "Lamin B Receptor" -> "Lamin B Receptor"

## Verified Verbatim Quotes
- "Lamin B receptor (LBR) is an inner nuclear membrane (INM) protein that plays crucial roles in maintaining nuclear architecture and organization of peripheral heterochromatin."
- "Lamins and LBR both contribute to chromatin tethering at the nuclear periphery, and the expression of LBR and A-type lamins is tightly regulated during development to ensure a faithful transition between different chromatin tethering modalities."
- "Here, we used mouse embryonic fibroblasts (MEFs) lacking all endogenous lamins (triple lamin knockout: TKO) to assess how specific lamin isoforms and domains regulate LBR subcellular localization and mobility."
- "Whereas ectopic expression of either lamin B1 or lamin B2 was sufficient to tether LBR to the nuclear envelope in TKO cells, expression of lamin A increased the lateral mobility of LBR at the nuclear membrane, resulting in its displacement from the nuclear envelope to the ER."
- "The lamin A-induced displacement of LBR was mediated by phosphorylation of LBR."
- "Overexpression of lamin A in wild-type MEFs similarly increased LBR phosphorylation and promoted its displacement from the nuclear envelope."
- "Collectively, these findings define isoform-specific and antagonistic roles for A-type and B-type lamins in regulating LBR anchorage at the nuclear envelope."
- "In addition, they indicate a lamin A-dependent mechanism that may reflect a broader developmental process, since LBR and lamin A sequentially tether peripheral heterochromatin during development."
- "Lamin B receptor (LBR) is an inner nuclear membrane protein that organizes peripheral heterochromatin and cooperates with lamins to tether chromatin at the nuclear periphery."
- "Expression of lamin B1 or B2 was sufficient to anchor LBR at the nuclear envelope, whereas lamin A expression increased LBR mobility and led to its displacement from the nuclear envelope."
- "This effect was mediated by phosphorylation of LBR and was recapitulated by lamin A overexpression in wild-type cells."
- "Histone deacetylases (HDACs) are important for global gene expression and contribute to numerous physiological events."
- "Inhibition of MTOR led to dephosphorylation and nucleo-cytoplasmic translocation of BmRpd3/HsHDAC1."
- "Besides, cholesterol, 20E, and 27-hydroxycholesterol could all induce massive dephosphorylation and cytoplasmic localization of BmRpd3/HsHDAC1, and thus autophagy by affecting MTORC1 activity."
- "In addition, three phosphorylation sites (Ser392, Ser421, and Ser423) identified in BmRpd3 were conserved in HsHDAC1."
- "Single or triple phosphorylation-site mutation attenuated the phosphorylation levels of BmRpd3/HsHDAC1, leading to their cytoplasmic localization and autophagy activation."
- "In general, cholesterol derivatives, especially hydroxylated cholesterol, caused dephosphorylation and nucleo-cytoplasmic shuttling of BmRpd3/HsHDAC1 through inhibition of MTOR signaling to facilitate autophagy in B. mori and mammals."
- "These findings improve our understandings of BmRpd3/HsHDAC1-mediated autophagy induced by cholesterol derivatives and shed light on their potential as a therapeutic target for neurodegenerative diseases and autophagy-related studies."
- "Despite its well-established association with B-type lamins, the contributions of individual lamin isoforms to LBR localization and anchorage have not been systematically examined."
- "Deacetylase Rpd3 in yeast and its conserved homolog HDAC1 in mammals oppositely regulate autophagy; however, how Rpd3/HDAC1 is regulated to mediate autophagy remains unclear."
- "Expression of lamin B1 or B2 was sufficient to anchor LBR at the nuclear envelope, whereas lamin A expression increased LBR mobility and led to its displacement from the nuclear envelope. This effect was mediated by phosphorylation of LBR"
- "Overexpression of lamin A in wild-type MEFs similarly increased LBR phosphorylation and promoted its displacement from the nuclear envelope."
- "One tether is constituted by the lamin B receptor (LBR) in mammals"
- "The lamin-B receptor (LBR) gene has two primary functions: maintaining the structural integrity of the nuclear envelope and playing a role in cholesterol biosynthesis."
- "LBR is a novel substrate of FBW7, which is degraded by GSK3β/FBW7-mediated proteasome pathway"
- "overexpression of this domain partially relocalized SRPK1 to the nucleus and resulted in hypophosphorylation of SR proteins, inhibition of splicing of a reporter minigene, and inhibition of Lamin B receptor phosphorylation."
- "lamin B receptor (LBR) partially redistributes from the nucleus to cytoplasm in mesoderm."
- "LBR depletion induces mitotic defects accompanied by recurrent chromosomal losses."
- "Emerin and lamin B receptor (LBR) are abundant transmembrane proteins of the nuclear envelope that are concentrated at the inner nuclear membrane (INM)."
- "localization and activity of the LBR-tether are crucially dependent on the muscle-specific chaperone HSPB3"
- "the disintegration of the lamin B receptor (LBR) and the collapse of the actin cytoskeleton occurs in early and later phases of NET release,"
- "packaging of nuclear DNA occurs in the lumen of nuclear envelope (NE)-derived multivesicular bodies (MVBs) that harbor the LTB 4 synthesizing machinery and is mediated by the lamin B receptor (LBR) and chromatin decondensation."
- "In the fruit fly Drosophila melanogaster, circadian rhythm was disrupted when the inner nuclear membrane protein lamin B receptor (LBR) was depleted from its clock neurons"
- "LBR likely facilitates PER foci accumulation by destabilizing the catalytic subunit of protein phosphatase 2A, MICROTUBULE STAR (MTS)."
- "Antinuclear envelope antibodies were detected in 65% of PBC patients"
- "interaction between nuclear membrane proteins such as LBR with heterochromatin modifications that are enriched in LADs chromatin."
- "MODY-associated mutations in HNF1A and HNF1B suppress mitochondrial function and interferon signaling"
- "LBR depletion phenocopies the effects of TOP2B depletion"
- "oligomeric tau (oTau) directly binds to the Lamin B Receptor (LBR), inducing nuclear envelope invaginations"
- "One tether is constituted by the lamin B receptor (LBR) in mammals"
- "Expression of lamin B1 or B2 was sufficient to anchor LBR at the nuclear envelope, whereas lamin A expression increased LBR mobility and led to its displacement from the nuclear envelope. This effect was mediated by phosphorylation of LBR"
- "Overexpression of lamin A in wild-type MEFs similarly increased LBR phosphorylation and promoted its displacement from the nuclear envelope."
- "The lamin-B receptor (LBR) gene has two primary functions: maintaining the structural integrity of the nuclear envelope and playing a role in cholesterol biosynthesis."
- "LBR is a novel substrate of FBW7, which is degraded by GSK3β/FBW7-mediated proteasome pathway"
- "overexpression of this domain partially relocalized SRPK1 to the nucleus and resulted in hypophosphorylation of SR proteins, inhibition of splicing of a reporter minigene, and inhibition of Lamin B receptor phosphorylation."
- "lamin B receptor (LBR) partially redistributes from the nucleus to cytoplasm in mesoderm."
- "LBR depletion induces mitotic defects accompanied by recurrent chromosomal losses."
- "Emerin and lamin B receptor (LBR) are abundant transmembrane proteins of the nuclear envelope that are concentrated at the inner nuclear membrane (INM)."
- "localization and activity of the LBR-tether are crucially dependent on the muscle-specific chaperone HSPB3"
- "the disintegration of the lamin B receptor (LBR) and the collapse of the actin cytoskeleton occurs in early and later phases of NET release,"
- "packaging of nuclear DNA occurs in the lumen of nuclear envelope (NE)-derived multivesicular bodies (MVBs) that harbor the LTB 4 synthesizing machinery and is mediated by the lamin B receptor (LBR) and chromatin decondensation."
- "In the fruit fly Drosophila melanogaster, circadian rhythm was disrupted when the inner nuclear membrane protein lamin B receptor (LBR) was depleted from its clock neurons"
- "LBR likely facilitates PER foci accumulation by destabilizing the catalytic subunit of protein phosphatase 2A, MICROTUBULE STAR (MTS)."
- "Antinuclear envelope antibodies were detected in 65% of PBC patients"
- "interaction between nuclear membrane proteins such as LBR with heterochromatin modifications that are enriched in LADs chromatin."
- "MODY-associated mutations in HNF1A and HNF1B suppress mitochondrial function and interferon signaling"
- "LBR depletion phenocopies the effects of TOP2B depletion"
- "oligomeric tau (oTau) directly binds to the Lamin B Receptor (LBR), inducing nuclear envelope invaginations"
- "One tether is constituted by the lamin B receptor (LBR) in mammals"
- "Expression of lamin B1 or B2 was sufficient to anchor LBR at the nuclear envelope, whereas lamin A expression increased LBR mobility and led to its displacement from the nuclear envelope. This effect was mediated by phosphorylation of LBR"
- "Overexpression of lamin A in wild-type MEFs similarly increased LBR phosphorylation and promoted its displacement from the nuclear envelope."
- "The lamin-B receptor (LBR) gene has two primary functions: maintaining the structural integrity of the nuclear envelope and playing a role in cholesterol biosynthesis."
- "LBR is a novel substrate of FBW7, which is degraded by GSK3β/FBW7-mediated proteasome pathway"
- "overexpression of this domain partially relocalized SRPK1 to the nucleus and resulted in hypophosphorylation of SR proteins, inhibition of splicing of a reporter minigene, and inhibition of Lamin B receptor phosphorylation."
- "lamin B receptor (LBR) partially redistributes from the nucleus to cytoplasm in mesoderm."
- "LBR depletion induces mitotic defects accompanied by recurrent chromosomal losses."
- "Emerin and lamin B receptor (LBR) are abundant transmembrane proteins of the nuclear envelope that are concentrated at the inner nuclear membrane (INM)."
- "localization and activity of the LBR-tether are crucially dependent on the muscle-specific chaperone HSPB3"
- "the disintegration of the lamin B receptor (LBR) and the collapse of the actin cytoskeleton occurs in early and later phases of NET release,"
- "packaging of nuclear DNA occurs in the lumen of nuclear envelope (NE)-derived multivesicular bodies (MVBs) that harbor the LTB 4 synthesizing machinery and is mediated by the lamin B receptor (LBR) and chromatin decondensation."
- "In the fruit fly Drosophila melanogaster, circadian rhythm was disrupted when the inner nuclear membrane protein lamin B receptor (LBR) was depleted from its clock neurons"
- "LBR likely facilitates PER foci accumulation by destabilizing the catalytic subunit of protein phosphatase 2A, MICROTUBULE STAR (MTS)."
- "Antinuclear envelope antibodies were detected in 65% of PBC patients"
- "interaction between nuclear membrane proteins such as LBR with heterochromatin modifications that are enriched in LADs chromatin."
- "MODY-associated mutations in HNF1A and HNF1B suppress mitochondrial function and interferon signaling"
- "LBR depletion phenocopies the effects of TOP2B depletion"
- "oligomeric tau (oTau) directly binds to the Lamin B Receptor (LBR), inducing nuclear envelope invaginations"
- "Structural prediction, molecular dynamics simulations, and biochemical analyses demonstrated that TagR exhibits the characteristic architecture of MarR family regulators and forms a stable homodimer."