Lamin dimers. Presence in the nuclear lamina of surf clam oocytes and release during nuclear envelope breakdown.

Dessev, George; Iovcheva-Dessev, Christina; Goldman, Robert D.

doi:10.1016/s0021-9258(19)38391-7

Cited by 27 publications

(6 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In living cells, cytosol and nucleoplasm are under reducing conditions due to a large pool of reduced glutathione. However, the nucleus contains the thioredoxin/thioredoxin reductase enzymes that catalyze the oxido/reduction of thiols (29), and disulfide bonds have been observed in proteins from the nuclear matrix (30) and in surf clam oocyte lamins (31). Cysteine 522 was not buried in LA/C (411-553) or in the larger lamin C fragment (411-572) (data not shown); thus, a disulfide bridge at this site may exist in ViVo.…”

Section: Discussionmentioning

confidence: 95%

The Carboxyl-Terminal Region Common to Lamins A and C Contains a DNA Binding Domain

et al. 2003

View full text Add to dashboard Cite

Lamins A and C are intermediate filament proteins which polymerize into the nucleus to form the nuclear lamina network. The lamina is apposed to the inner nuclear membrane and functions in tethering chromatin to the nuclear envelope and in maintaining nuclear shape. We have recently characterized a globular domain that adopts an immunoglobulin fold in the carboxyl-terminal tail common to lamins A and C. Using an electrophoretic mobility shift assay (EMSA), we show that a peptide containing this domain interacts in vitro with DNA after dimerization through a disulfide bond, but does not interact with the core particle or the dinucleosome. The covalent dimer binds a 30-40 bp DNA fragment with a micromolar affinity and no sequence specificity. Using nuclear magnetic resonance (NMR) and an EMSA, we observed that two peptide regions participate in the DNA binding: the unstructured amino-terminal part containing the nuclear localization signal and a large positively charged region centered around amino acid R482 at the surface of the immunoglobulin-like domain. Mutations R482Q and -W, which are responsible for Dunnigan-type partial lipodystrophy, lower the affinity of the peptide for DNA. We conclude that the carboxyl-terminal end of lamins A and C binds DNA and suggest that alterations in lamin-DNA interactions may play a role in the pathophysiology of some lamin-linked diseases.

show abstract

Section: Discussionmentioning

confidence: 95%

The Carboxyl-Terminal Region Common to Lamins A and C Contains a DNA Binding Domain

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Disassembly of lamins is required for nuclear envelope breakdown in the early stage of mitosis. Plenty of studies revealed that this process was dominated by lamin phosphorylation under the catalysis of Cdk1 ( Dessev et al, 1990 ; Heald and McKeon, 1990 ; Peter et al, 1990 ; Mall et al, 2012 ). Moreover, phosphorylated lamin A/C is released into the cytoplasm, while phosphorylated farnesylated B-type lamins remain membrane bound but disperse throughout the ER during mitosis ( Gerace et al, 1984 ; Georgatos et al, 1997 ).…”

Section: Phosphorylation: Multifunctional Post-translational Modifica...mentioning

confidence: 99%

Post-Translational Modification of Lamins: Mechanisms and Functions

Zheng

Jin

Zhou

2022

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

Lamins are the ancient type V intermediate filament proteins contributing to diverse biological functions, such as the maintenance of nuclear morphology, stabilization of chromatin architecture, regulation of cell cycle progression, regulation of spatial-temporal gene expressions, and transduction of mechano-signaling. Deregulation of lamins is associated with abnormal nuclear morphology and chromatin disorganization, leading to a variety of diseases such as laminopathy and premature aging, and might also play a role in cancer. Accumulating evidence indicates that lamins are functionally regulated by post-translational modifications (PTMs) including farnesylation, phosphorylation, acetylation, SUMOylation, methylation, ubiquitination, and O-GlcNAcylation that affect protein stabilization and the association with chromatin or associated proteins. The mechanisms by which these PTMs are modified and the relevant functionality become increasingly appreciated as understanding of these changes provides new insights into the molecular mechanisms underlying the laminopathies concerned and novel strategies for the management. In this review, we discussed a range of lamin PTMs and their roles in both physiological and pathological processes, as well as potential therapeutic strategies by targeting lamin PTMs.

show abstract

“…When considering possible determinants conferring membrane affinity to B-type lamins, it is noteworthy that B-as well as A-type lamins readily form dimers, and that even in their mitotically disassembled state they may exist as dimers or tetramers (Gerace and Blobel, 1980;Havre and Evans, 1983;Benavente et al, 1985;Aebi et al, 1986;Krohne et al, 1987;Dessev et al, 1990;Heitlinger et al, 1991).If this is the ease, each lamin oligomer would be held at the membrane by at least two isoprene substitutents, and overall avidity for the nuclear membrane would be substantially increased. An alternative explanation for thepreferential membrane attachment of B-type lamin proteins is suggested by studies describing integral membrane proteins that may function as receptors for B-type lamins (Worman et al, 1988; see also Senior and Gerace, 1988;Padan et al, 1990).…”

Section: What Is the Molecular Function Of Caax Box Modification Of Lamin Proteins ?mentioning

confidence: 99%

The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2.

Kitten

Nigg

1991

The Journal of Cell Biology

183

120

View full text Add to dashboard Cite

Abstract. Recent evidence suggests that the conserved COOH-terminal CaaX motif of nuclear lamins may play a role in targeting newly synthesized proteins to the nuclear envelope. We have shown previously that in rabbit reticulocyte lysates the cysteine residue of the CaaX motif of chicken lamin B2 is necessary for incorporation of a derivative of mevalonic acid, the precursor of isoprenoids. Here we have analyzed the properties of normal and mutated forms of chicken lamin B2 stably expressed in mouse L cells. Mutation of the cysteine residue of the CaaX motif to alanine or introduction of a stop codon immediately after the cysteine residue was found to abolish both isoprenylation and carboxyl methylation of transfected lamin B2. Concomitantly, although nuclear import of the mutant lamin B2 proteins was preserved, their association with the inner nuclear membrane was severely impaired. From these results we conclude that the COOH-terminal CaaX motif is required for isoprenylation and carboxyl methylation of lamins in vivo, and that these modifications are important for association of B-type lamins with the nucleoplasmic surface of the inner nuclear membrane.

show abstract

Lamin dimers. Presence in the nuclear lamina of surf clam oocytes and release during nuclear envelope breakdown.

Cited by 27 publications

References 32 publications

The Carboxyl-Terminal Region Common to Lamins A and C Contains a DNA Binding Domain

The Carboxyl-Terminal Region Common to Lamins A and C Contains a DNA Binding Domain

Post-Translational Modification of Lamins: Mechanisms and Functions

The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2.

Contact Info

Product

Resources

About