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Cited by 295

The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.

Rac/Cdc42 and p65PAK Regulate the Microtubule-destabilizing Protein Stathmin through Phosphorylation at Serine 16

Open access
Daub, Henrik, Gevaert, Kris, Vandekerckhove, Joel, Sobel, André, Hall, Alan·2001·Journal of Biological Chemistry

Abstract

We have identified a rapid protein phosphorylation event at residue serine 16 of stathmin using two-dimensional gel electrophoresis coupled to matrix-assisted laser desorption/ionization mass spectrometry in combination with post-source decay analysis, which is induced by the epidermal growth factor receptor. Phosphorylation is specifically mediated by the small GTPases Rac and Cdc42 and their common downstream target, the serine/threonine kinase p65PAK. Both GTPases have previously been shown to regulate the dynamics of actin polymerization. Because stathmin destabilizes microtubules, and this process is inhibited by phosphorylation at residue 16, Rac and Cdc42 can potentially regulate both F-actin and microtubule dynamics.

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Metadata

Authors
Daub, H., Gevaert, K., Vandekerckhove, J., Sobel, A., & Hall, A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-01
Volume
276
Issue
3
Pages
1677-1680
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2017328399
Cited by
295
References
20
FWCI
7.86
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Rac/Cdc42 and p65PAK Regulate the Microtubule-destabilizing Protein Stathmin through Phosphorylation at Serine 16. https://app.cochat.ai/papers/10.1074/jbc.c000635200
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Daub, H., Gevaert, K., Vandekerckhove, J., Sobel, A., & Hall, A. (2001). Rac/Cdc42 and p65PAK Regulate the Microtubule-destabilizing Protein Stathmin through Phosphorylation at Serine 16. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.c000635200

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