Coordination of Kinase and Phosphatase Activities by Lem4 Enables Nuclear Envelope Reassembly during Mitosis

Asencio, Claudio; Davidson, Iain F.; Santarella-Mellwig, Rachel; Ly-Hartig, Thi Bach Nga; Mall, Moritz; Wallenfang, Matthew R.; Mattaj, Iain W.; Gorjánácz, Mátyás

doi:10.1016/j.cell.2012.04.043

Cited by 152 publications

(228 citation statements)

References 44 publications

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“…Of note, unlike its human homolog, LEM-4 has neither a LEM domain nor a transmembrane domain, and hence it is considered a LEM4-like protein. Antibodies against LEM-4 revealed that it is enriched at the NE (Asencio et al 2012). What regulates LEM-4 so that it desphosphorylates BAF-1 only when chromosome segregation is completed is an interesting and unresolved question.…”

Section: Ne Reassemblymentioning

confidence: 99%

“…BAF-1 is phosphorylated by the VRK-1 kinase (Gorjanacz et al 2007) and this reduces its affinity to DNA. This phosphorylation is reversed by the PP2A phosphatase (Asencio et al 2012).…”

Section: Components Of the Nementioning

confidence: 99%

“…To promote NE detachment from chromatin, BAF-1 is phosphorylated by VRK-1 (Gorjanacz et al 2007). To overcome this VRK-1-dependent phosphorylation of BAF-1, LEM-4, a protein homologous to the human LEM4/ANKLE2, recruits the PP2A phosphatase, which dephosphorylates BAF-1 to allow NE reassembly (Asencio et al 2012). LEM-4 also inhibits VRK-1's kinase activity (Asencio et al 2012).…”

Section: Ne Reassemblymentioning

confidence: 99%

“…To overcome this VRK-1-dependent phosphorylation of BAF-1, LEM-4, a protein homologous to the human LEM4/ANKLE2, recruits the PP2A phosphatase, which dephosphorylates BAF-1 to allow NE reassembly (Asencio et al 2012). LEM-4 also inhibits VRK-1's kinase activity (Asencio et al 2012). Of note, unlike its human homolog, LEM-4 has neither a LEM domain nor a transmembrane domain, and hence it is considered a LEM4-like protein.…”

Section: Ne Reassemblymentioning

confidence: 99%

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Cell Biology of theCaenorhabditis elegansNucleus

Cohen-Fix

Askjaer

2017

Genetics

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Studies on the Caenorhabditis elegans nucleus have provided fascinating insight to the organization and activities of eukaryotic cells. Being the organelle that holds the genetic blueprint of the cell, the nucleus is critical for basically every aspect of cell biology. The stereotypical development of C. elegans from a one cell-stage embryo to a fertile hermaphrodite with 959 somatic nuclei has allowed the identification of mutants with specific alterations in gene expression programs, nuclear morphology, or nuclear positioning. Moreover, the early C. elegans embryo is an excellent model to dissect the mitotic processes of nuclear disassembly and reformation with high spatiotemporal resolution. We review here several features of the C. elegans nucleus, including its composition, structure, and dynamics. We also discuss the spatial organization of chromatin and regulation of gene expression and how this depends on tight control of nucleocytoplasmic transport. Finally, the extensive connections of the nucleus with the cytoskeleton and their implications during development are described. Most processes of the C. elegans nucleus are evolutionarily conserved, highlighting the relevance of this powerful and versatile model organism to human biology.KEYWORDS Caenorhabditis elegans; chromatin; gene expression; lamin; LEM-domain proteins; LINC; P granule; nuclear pore complex; nuclear envelope; nucleocytoplasmic transport; nucleolus; WormBook TABLE OF CONTENTSAbstract 25 C. elegans as a model system to study cell biology of the nucleus 26 Structural components of the nucleus 27

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Section: Ne Reassemblymentioning

confidence: 99%

“…BAF-1 is phosphorylated by the VRK-1 kinase (Gorjanacz et al 2007) and this reduces its affinity to DNA. This phosphorylation is reversed by the PP2A phosphatase (Asencio et al 2012).…”

Section: Components Of the Nementioning

confidence: 99%

Section: Ne Reassemblymentioning

confidence: 99%

Section: Ne Reassemblymentioning

confidence: 99%

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Cell Biology of theCaenorhabditis elegansNucleus

Cohen-Fix

Askjaer

2017

Genetics

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“…The NE contains many integral proteins (23-26) that participate in genome management or NE reassembly (25,27,28). Emerin is a NE inner membrane protein that interacts with A-and B-type lamins to mediate the anchorage of NE to cytoskeleton (29) and to regulate gene transcription by binding to other chromatin-remodeling molecules such as β-catenin or barrier-to-autointegration factor…”

mentioning

confidence: 99%

Sigma-1 receptor mediates cocaine-induced transcriptional regulation by recruiting chromatin-remodeling factors at the nuclear envelope

Tsai

Chuang

Tsai

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

115

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The sigma-1 receptor (Sig-1R) chaperone at the endoplasmic reticulum (ER) plays important roles in cellular regulation. Here we found a new function of Sig-1R, in that it translocates from the ER to the nuclear envelope (NE) to recruit chromatin-remodeling molecules and regulate the gene transcription thereof. Sig-1Rs mainly reside at the ER-mitochondrion interface. However, on stimulation by agonists such as cocaine, Sig-1Rs translocate from ER to the NE, where Sig-1Rs bind NE protein emerin and recruit chromatin-remodeling molecules, including lamin A/C, barrier-to-autointegration factor (BAF), and histone deacetylase (HDAC), to form a complex with the gene repressor specific protein 3 (Sp3). Knockdown of Sig-1Rs attenuates the complex formation. Cocaine was found to suppress the gene expression of monoamine oxidase B (MAOB) in the brain of wild-type but not Sig-1R knockout mouse. A single dose of cocaine (20 mg/kg) in rats suppresses the level of MAOB at nuclear accumbens without affecting the level of dopamine transporter. Daily injections of cocaine in rats caused behavioral sensitization. Withdrawal from cocaine in cocaine-sensitized rats induced an apparent time-dependent rebound of the MAOB protein level to about 200% over control on day 14 after withdrawal. Treatment of cocaine-withdrawn rats with the MAOB inhibitor deprenyl completely alleviated the behavioral sensitization to cocaine. Our results demonstrate a role of Sig-1R in transcriptional regulation and suggest cocaine may work through this newly discovered genomic action to achieve its addictive action. Results also suggest the MAOB inhibitor deprenyl as a therapeutic agent to block certain actions of cocaine during withdrawal.T he endoplasmic reticulum (ER) plays important roles in cellular functions, including synthesis of proteins and regulation of Ca 2+ signaling between the ER and plasma membrane (1) and between the ER and mitochondria (2-4). However, because the ER interacts with other organelles in the cell, other functions related to the ER remain to be uncovered.The sigma-1 receptor (Sig-1R) (5-8) is an ER chaperone molecule that resides at the ER-mitochondrion interface referred to as the mitochondria-associated ER membrane (MAM), where the Sig-1R ensures proper ER-mitochondrion Ca 2+ signaling for cellular survival (3, 9), as well as sustains the activity of an ER stress sensor IRE1 at the MAM (10). The Sig-1R can translocate from the MAM to plasma membrane of the cell to regulate ion channels and receptors on the plasma membrane (8,(11)(12)(13)(14). Cocaine is a Sig-1R agonist (3) that causes the dissociation of Sig-1R from its cognate binding partner BiP (3,8), and consequently the translocation of Sig-1Rs to the plasma membrane, where Sig-1Rs interact with voltage-gated potassium channel subfamily A member 2 (Kv1.2) to shape the neuronal and behavioral responses to cocaine (15).Cocaine also causes the translocation of Sig-1Rs from the ER to the nucleus (16), where Sig-1Rs are shown to be present at the nuclear envelope (NE) (17). H...

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The secret life of chromatin tethers

Kiseleva

Poleshko

2023

FEBS Letters

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The nuclear envelope plays an essential role in organizing the genome inside of the nucleus. The inner nuclear membrane is coated with a meshwork of filamentous lamin proteins that provide a surface to organize a variety of cellular processes. A subset of nuclear lamina‐ and membrane‐associated proteins functions as anchors to hold transcriptionally silent heterochromatin at the nuclear periphery. While most chromatin tethers are integral membrane proteins, a limited number are lamina‐bound. One example is the mammalian proline‐rich 14 (PRR14) protein. PRR14 is a recently characterized protein with unique function that is different from other known chromatin tethers. Here, we review our current understanding of PRR14 structure and function in organizing heterochromatin at the nuclear periphery.

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Coordination of Kinase and Phosphatase Activities by Lem4 Enables Nuclear Envelope Reassembly during Mitosis

Cited by 152 publications

References 44 publications

Cell Biology of theCaenorhabditis elegansNucleus

Cell Biology of theCaenorhabditis elegansNucleus

Sigma-1 receptor mediates cocaine-induced transcriptional regulation by recruiting chromatin-remodeling factors at the nuclear envelope

The secret life of chromatin tethers

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