The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Inhibition of Myosin Light Chain Kinase by p21-Activated Kinase
Abstract
p21-activated kinases (PAKs) are implicated in the cytoskeletal changes induced by the Rho family of guanosine triphosphatases. Cytoskeletal dynamics are primarily modulated by interactions of actin and myosin II that are regulated by myosin light chain kinase (MLCK)–mediated phosphorylation of the regulatory myosin light chain (MLC). p21-activated kinase 1 (PAK1) phosphorylates MLCK, resulting in decreased MLCK activity. MLCK activity and MLC phosphorylation were decreased, and cell spreading was inhibited in baby hamster kidney–21 and HeLa cells expressing constitutively active PAK1. These data indicate that MLCK is a target for PAKs and that PAKs may regulate cytoskeletal dynamics by decreasing MLCK activity and MLC phosphorylation.
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Citations
Cites
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Self-citationHuman p21-activated kinase (Pak1) regulates actin organization in mammalian cells
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Cited by
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Cell migration: Rho GTPases lead the way
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Metadata
- Authors
- Sanders, L. C., Matsumura, F., Bokoch, G. M., & de Lanerolle, P.
- Venue
- Science
- Published
- 1999-03-26
- Volume
- 283
- Issue
- 5410
- Pages
- 2083-2085
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1986349419
- Cited by
- 593
- References
- 19
- FWCI
- 19.36
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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