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Article

Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2.

The Journal of cell biology - 27 Dec 1999

Sumi T, Matsumoto K, Takai Y, Nakamura T

Abstract excerpt

The rapid turnover of actin filaments and the tertiary meshwork formation are regulated by a variety of actin-binding proteins. Protein phosphorylation of cofilin, an actin-binding protein that depolymerizes actin filaments, suppresses its function. Thus, cofilin is a terminal effector of signaling cascades that evokes actin cytoskeletal rearrangement. When wild-type LIMK2 and kinase-dead LIMK2 (LIMK2/KD) were...

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Share to Actin Depolymerizing Factors
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 10613909
DOI: 10.1083/jcb.147.7.1519
PMCID: PMC2174243

Genes

LIMK2
LIMK1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2.PMID 10613909Read ↗

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The Role of LIM Kinase in the Male Urogenital SystemSemantic proximity Read ↗

Keratinocyte migration in the developing eyelid requires LIMK2.Semantic proximity Read ↗

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