Lamin-binding Proteins

Overview

Journal Cold Spring Harb Perspect Biol

Specialties Biology
Molecular Biology

Date 2010 May 11

PMID 20452940

Citations 154

Authors

Katherine L Wilson

Roland Foisner

Affiliations

Soon will be listed here.

Abstract

A- and B-type lamins are the major intermediate filaments of the nucleus. Lamins engage in a plethora of stable and transient interactions, near the inner nuclear membrane and throughout the nucleus. Lamin-binding proteins serve an amazingly diverse range of functions. Numerous inner-membrane proteins help anchor lamin filaments to the nuclear envelope, serving as part of the nuclear "lamina" network that is essential for nuclear architecture and integrity. Certain lamin-binding proteins of the inner membrane bind partners in the outer membrane and mechanically link lamins to the cytoskeleton. Inside the nucleus, lamin-binding proteins appear to serve as the "adaptors" by which the lamina organizes chromatin, influences gene expression and epigenetic regulation, and modulates signaling pathways. Transient interactions of lamins with key components of the transcription and replication machinery may provide an additional level of regulation or support to these essential events.

Citing Articles

Lamin chromatin binding is modulated by interactions of different LAP2α domains with lamins and chromatin.

Filipczak D, Souchet A, Georgiou K, Foisner R, Naetar N iScience. 2024; 27(10):110869.

PMID: 39319273 PMC: 11417337. DOI: 10.1016/j.isci.2024.110869.

Nuclear lamin A/C phosphorylation by loss of androgen receptor leads to cancer-associated fibroblast activation.

Ghosh S, Isma J, Ostano P, Mazzeo L, Toniolo A, Das M Nat Commun. 2024; 15(1):7984.

PMID: 39266569 PMC: 11392952. DOI: 10.1038/s41467-024-52344-z.

Cyclic stretch induced epigenetic activation of periodontal ligament cells.

Bae H, Shin S, Jo S, Li C, Lee D, Lee J Mater Today Bio. 2024; 26:101050.

PMID: 38654935 PMC: 11035113. DOI: 10.1016/j.mtbio.2024.101050.

Nesprin proteins: bridging nuclear envelope dynamics to muscular dysfunction.

Zi-Yi Z, Qin Q, Fei Z, Cun-Yu C, Lin T Cell Commun Signal. 2024; 22(1):208.

PMID: 38566066 PMC: 10986154. DOI: 10.1186/s12964-024-01593-y.

PIGB maintains nuclear lamina organization in skeletal muscle of Drosophila.

Yamamoto-Hino M, Ariura M, Tanaka M, Iwasaki Y, Kawaguchi K, Shimamoto Y J Cell Biol. 2024; 223(2).

PMID: 38261271 PMC: 10808031. DOI: 10.1083/jcb.202301062.

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