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First published online September 9, 2005
doi: 10.1242/10.1242/jcs.02557
Research Article |
1 Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK
2 Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
* Author for correspondence (e-mail: c.j.weijer{at}dundee.ac.uk)
Accepted 22 June 2005
Paxillin is a key regulatory component of focal adhesion sites, implicated in controlling cell-substrate interactions and cell movement. We analyse the function of aDictyostelium discoideumpaxillin homologue, PaxB, which contains four highly conserved LD and four LIM domains, but lacks two characteristic tyrosine residues, that form the core of vertebrate SH2-binding domains. PaxB is expressed during growth and all stages of development, but expression peaks during slug formation. Using apaxB-gfpknockin strain we show the existence of focal adhesions and characterise their dynamics. During multicellular development PaxB is not only found in focal adhesions at the cell-substrate interface, but also in the tips of filopodial structures predominantly located at the trailing ends of cells.paxBstrains are less adhesive to the substrate, they can aggregate but multicellular development from the mound stage onwards is severely impeded.paxB strains are defective in proper cell type proportioning, cell sorting, slug migration and form-defective fruiting bodies. Mutation of a conserved JNK phosphorylation site, implicated in the control of cell migration, does not have any major effects on cell sorting, slug migration or morphogenesis inDictyostelium. PaxB does not appear to function redundantly with its closest relative Lim2 (paxA), which when deleted also results in a mound arrest phenotype. However, analysis ofpaxAandpaxBsingle and double null mutants suggest that PaxB may act upstream of Lim2.
Key words: Paxillin, Cell motility, Chemotaxis, Sorting, Morphogenesis, Signalling
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