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EMBO reports 5, 2, 154–160 (2004)
doi:10.1038/sj.embor.7400079
AOP Published online: 23 January 2004
p41-Arc subunit of human Arp2/3 complex is a p21-activated kinase-1-interacting substrate
Ratna K Vadlamudi, Feng Li, Christopher J Barnes, Rozita Bagheri-Yarmand & Rakesh Kumar
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Department of Molecular and Cellular Oncology,
The University of Texas MD Anderson Cancer Center, 1515 Holcombe
Boulevard, Houston, Texas 77030,
USA
To whom correspondence should be addressed
Rakesh Kumar Tel: +1 713 745 3558; Fax: +1 713 745 3792; E-mail:
rkumar@mdanderson.org
Received 19 February 2003; Accepted 5 December 2003; Published online 23 January 2004.
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Abstract
The formation of new branched actin filament networks at the cell
cortex of migrating cells is choreographed by the actin-related protein (Arp)
2/3 complex. Despite the fundamental role of the Arp2/3 complex in actin
nucleation and branching, upstream signals that control the functions of
p41-Arc, a putative regulatory component of the mammalian Arp2/3 complex,
remain unidentified. Here we show that p41-Arc interacts with p21-activated
kinase 1 (Pak1) both in vitro and in vivo. Pak1 phosphorylation
of p41-Arc regulates its localization with the Arp2/3 complex in the cortical
nucleation regions of cells. Pak1 phosphorylates p41-Arc on threonine 21 in the
first WD repeat, and its mutation has functional implications in vivo.
Threonine 21 phosphorylation by Pak1 is required for both constitutive and
growth-factor-induced cell motility. Pak1 regulation of p41-Arc activation
status represents a novel mechanism by which signalling pathways may influence
the functions of the Arp2/3 complex, leading to motility in mammalian
cells.
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