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- W2065609541 endingPage "18091" @default.
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- W2065609541 abstract "Sterile 20 (STE20) protein kinases, which include germinal center kinases and p21-activated protein kinases, are known to activate mitogen-activated protein kinase pathways (c-Jun NH2-terminal kinase, p38, or extracellular signal-regulated kinase), leading to changes in gene transcription. Some STE20s can also regulate the cytoskeleton, and we have shown that the germinal center kinase-like kinase prostate-derived STE20-like kinase (PSK) affects actin cytoskeletal organization. Here, we demonstrate that PSK colocalizes with microtubules; and that this localization is disrupted by the microtubule depolymerizing agent nocodazole. The association of PSK with microtubules results in the production of stabilized perinuclear microtubule cables that are nocodazole-resistant and contain increased levels of acetylated α-tubulin. Kinase-defective PSK (K57A) or the C terminus of PSK (amino acids 745–1235) lacking the kinase domain are sufficient for microtubule binding and stabilization, demonstrating that the catalytic activity of the protein is not required. The localization of PSK to microtubules occurs via its C terminus, and PSK binds and phosphorylates α- and β-tubulin in vitro. The N terminus of PSK (1–940) is unable to bind or stabilize microtubules, demonstrating that PSK must associate with microtubules for their reorganization to occur. These results demonstrate that PSK interacts with microtubules and affects their organization and stability independently of PSK kinase activity." @default.
- W2065609541 created "2016-06-24" @default.
- W2065609541 creator A5010230447 @default.
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- W2065609541 date "2003-05-01" @default.
- W2065609541 modified "2023-10-02" @default.
- W2065609541 title "The Prostate-derived Sterile 20-like Kinase (PSK) Regulates Microtubule Organization and Stability" @default.
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- W2065609541 doi "https://doi.org/10.1074/jbc.m213064200" @default.
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