The multi-FERM-domain-containing protein FrmA is required for turnover of paxillin-adhesion sites during cell migration of Dictyostelium
Author:
Patel Hitesh1, König Ireen1, Tsujioka Masatsune2, Frame Margaret C.1, Anderson Kurt I.1, Brunton Valerie G.1
Affiliation:
1. The Beatson Institute for Cancer Research, Garscube Estate, Switchback Road, Bearsden, Glasgow, G61 1BD, UK 2. RIKEN, Center for Developmental Biology, 2-2-3 Minatojima-minamimachi, Chuo-ku, Kobe 650-0047, Japan
Abstract
FERM domain proteins, including talins, ERMs, FAK and certain myosins, regulate connections between the plasma membrane, cytoskeleton and extracellular matrix. Here we show that FrmA, a Dictyostelium discoideum protein containing two talin-like FERM domains, plays a major role in normal cell shape, cell-substrate adhesion and actin cytoskeleton organisation. Using total internal reflection fluorescence (TIRF) microscopy we show that FrmA-null cells are more adherent to substrate than wild-type cells because of an increased number, persistence and mislocalisation of paxillin-rich cell-substrate adhesions, which is associated with decreased motility. We show for the first time that talinA colocalises with paxillin at the distal ends of filopodia to form cell-substrate adhesions and indeed arrives prior to paxillin. After a period of colocalisation, talin leaves the adhesion site followed by paxillin. Whereas talinA-rich spots turnover prior to the arrival of the main body of the cell, paxillin-rich spots turn over as the main body of the cell passes over it. In FrmA-null cells talinA initially localises to cell-substrate adhesion sites at the distal ends of filopodia but paxillin is instead localised to stabilised adhesion sites at the periphery of the main cell body. This suggests a model for cell-substrate adhesion in Dictyostelium whereby the talin-like FERM domains of FrmA regulate the temporal and spatial control of talinA and paxillin at cell-substrate adhesion sites, which in turn controls adhesion and motility.
Publisher
The Company of Biologists
Reference19 articles.
1. Bretschneider, T., Diez, S., Anderson, K., Heuser, J., Clarke, M., Muller-Taubenberger, A., Kohler, J. and Gerisch, G. (2004). Dynamic actin patterns and Arp2/3 assembly at the substrate-attached surface of motile cells. Curr. Biol.14, 1-10. 2. Bukharova, T., Weijer, G., Bosgraaf, L., Dormann, D., van Haastert, P. J. and Weijer, C. J. (2005). Paxillin is required for cell-substrate adhesion, cell sorting and slug migration during Dictyostelium development. [erratum appears in J. Cell Sci. 2005 Oct 15; 118 (Pt 20): 4913 Note: Bukahrova, Tanya [corrected to Bukhavora, Tanya]]. J. Cell Sci.118, 4295-4310. 3. Diakowski, W., Grzybek, M. and Sikorski, A. F. (2006). Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily. Folia Histochem. Cytobiol.44, 231-248. 4. Fey, P., Stephens, S., Titus, M. A. and Chisholm, R. L. (2002). SadA, a novel adhesion receptor in Dictyostelium. J. Cell Biol.159, 1109-1119. 5. Gerisch, G., Bretschneider, T., Muller-Taubenberger, A., Simmeth, E., Ecke, M., Diez, S. and Anderson, K. (2004). Mobile actin clusters and traveling waves in cells recovering from actin depolymerization. Biophys. J.87, 3493-3503.
Cited by
20 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|