Paxillin associates with Poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells

Woods, Alison J, Roberts, Marnie S, Choudhary, Jyoti, Barry, Simon T, Mazaki, Yuichi, Sabe, Hisataka, Morley, Simon, Critchley, David R and Norman, Jim C (2002) Paxillin associates with Poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells. Journal of Biological Chemistry, 277 (8). pp. 6428-6437. ISSN 0021-9258

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Abstract

Using mass spectrometry we have identified proteins which co-immunoprecipitate with paxillin, an adaptor protein implicated in the integrin-mediated signaling pathways of cell motility. A major component of paxillin immunoprecipitates was poly(A)-binding protein 1, a 70-kDa mRNA-binding protein. Poly(A)-binding protein 1 associated with both the a and ß isoforms of paxillin, and this was unaffected by RNase treatment consistent with a protein-protein interaction. The NH2-terminal region of paxillin (residues 54¿313) associated directly with poly(A)-binding protein 1 in cell lysates, and with His-poly(A)-binding protein 1 immobilized in microtiter wells. Binding was specific, saturable and of high affinity (K d of ¿10 nm). Cell fractionation studies showed that at steady state, the bulk of paxillin and poly(A)-binding protein 1 was present in the ¿dense¿ polyribosome-associated endoplasmic reticulum. However, inhibition of nuclear export with leptomycin B caused paxillin and poly(A)-binding protein 1 to accumulate in the nucleus, indicating that they shuttle between the nuclear and cytoplasmic compartments. When cells migrate, poly(A)-binding protein 1 colocalized with paxillin-ß at the tips of lamellipodia. Our results suggest a new mechanism whereby a paxillipoly(A)-binding protein 1 complex facilitates transport of mRNA from the nucleus to sites of protein synthesis at the endoplasmic reticulum and the leading lamella during cell migration.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: EPrints Services
Date Deposited: 06 Feb 2012 19:59
Last Modified: 30 Jul 2019 07:58
URI: http://sro.sussex.ac.uk/id/eprint/23393
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