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Publication : Pak1 and its T212 phosphorylated form accumulate in neurones and epithelial cells of the developing rodent.

First Author  Zhong JL Year  2003
Journal  Dev Dyn Volume  228
Issue  1 Pages  121-7
PubMed ID  12950086 Mgi Jnum  J:85489
Mgi Id  MGI:2675518 Doi  10.1002/dvdy.10351
Citation  Zhong JL, et al. (2003) Pak1 and its T212 phosphorylated form accumulate in neurones and epithelial cells of the developing rodent. Dev Dyn 228(1):121-7
abstractText  The serine/threonine kinase Pak1 is a target of the RhoGTPases Rac and Cdc42 and an important regulator of cell morphology and migration. Recent work from several laboratories has indicated that Pak1 controls microtubule dynamics as well as the organisation of F-actin microfilaments. Pak1 is phosphorylated on T212 by the p35/Cdk5 or cyclin B1/Cdc2 kinase in postmitotic neurones and mitotic cells, respectively. To understand its function during development, we have carried out a detailed temporal and spatial analysis of Pak1 expression and phosphorylation on T212. In the embryonic forebrain, Pak1 and Pak1T212(PO4) were seen to accumulate in the corpus callosum, intermediate zone, lateral olfactory tracts, and anterior commissures. Epithelial cells of the mouse embryo lung, kidney, intestine, and skin also exhibited high levels of Pak1 and Pak1T212(PO4), suggesting a previously unsuspected role in epithelial differentiation. Pak1T212(PO4) was undetectable in all adult tissues. Together, these data indicate a specific, developmentally regulated role of the Pak1 kinase.
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