Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
Article Abstract:
LIM-kinase 1 (LIMK-1), a serine/threonine kinase containing LIM and PDZ domains, plays a role in Rac-mediated actin cytoskeletal reorganization. There is a potential connection between Rac, LIMK-1, cofilin and actin-filament dynamics. Rac prompts the kinase activity of LIMK-1, which in turn leads to phosphorylation and inactivation of cofilin. It probably also prompts a fall in the rate of actin depolymerization. LIMK-1 activity may be localized to confined regions within the cell by the binding of LIMK-1 to F-actin.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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CRM 1 is responsible for intracellular transport mediated by the nuclear export signal
Article Abstract:
Cellular research demonstrates that nuclear export signal (NES) proteins are inhibited by the cytotoxin leptomycin B. The Xenopus oocyte protein p110 which specifically binds to intact NES has been identified as the evolutionarily conserved protein CRM1. Evidence suggests that CRM1 is crucial to the nuclear export of proteins in the cells of multicellular organisms.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Polo-like kinase 1 phosphorylates cyclin B1 and targets it to the nucleus during prophase
Article Abstract:
Research is presented concerning the purification of the protein kinase from M-phase extracts of Xenopus which phosphorylates a serine residue half way through the nuclear export signal sequence.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2001
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