Abstract:
:We have previously identified poly(A)-binding protein 1 (PABP1) as a ligand for paxillin and shown that the paxillin-PABP1 complex undergoes nucleocytoplasmic shuttling. By targeting the paxillin-binding subdomain sequences in PABP1, we have generated mutants of PABP1 that do not bind to cellular paxillin. Here we report that paxillin association is necessary for efficient nuclear export of PABP1 and that RNA interference of paxillin drives the nuclear accumulation of PABP1. Furthermore, ablation of paxillin-PABP1 association impeded a number of indices of cell motility including spreading on fibronectin, cell migration on two-dimensional matrices, and transmigration in Boyden chambers. These data indicate that PABP1 must associate with paxillin in order to be efficiently transported from the nucleus to the cytoplasm and that this event is necessary for cells to remodel their focal adhesions during cell migration.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Woods AJ,Kantidakis T,Sabe H,Critchley DR,Norman JCdoi
10.1128/MCB.25.9.3763-3773.2005subject
Has Abstractpub_date
2005-05-01 00:00:00pages
3763-73issue
9eissn
0270-7306issn
1098-5549pii
25/9/3763journal_volume
25pub_type
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