Increased filamin binding to beta-integrin cytoplasmic domains inhibits cell migration. Export

@article{citeulike:6032131, abstract = {Multicellular animal development depends on integrins. These adhesion receptors link to the actin cytoskeleton, transmitting biochemical signals and force during cell migration and interactions with the extracellular matrix. Many integrin-cytoskeleton connections are formed by filamins and talin. The beta7 integrin tail binds strongly to filamin and supports less migration, fibronectin matrix assembly and focal adhesion formation than either the beta1D tail, which binds strongly to talin, or the beta1A tail, which binds modestly to both filamin and talin. To probe the role of filamin binding, we mapped the filamin-binding site of integrin tails and identified amino acid substitutions that led to selective loss of filamin binding to the beta7 tail and gain of filamin binding to the beta1A tail. These changes affected cell migration and membrane protrusions but not fibronectin matrix assembly or focal adhesion formation. Thus, tight filamin binding restricts integrin-dependent cell migration by inhibiting transient membrane protrusion and cell polarization.}, author = {Calderwood, D. A. and Huttenlocher, A. and Kiosses, W. B. and Rose, D. M. and Woodside, D. G. and Schwartz, M. A. and Ginsberg, M. H.}, citeulike-article-id = {6032131}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/ncb1201-1060}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11781567}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11781567}, doi = {10.1038/ncb1201-1060}, issn = {1465-7392}, journal = {Nature cell biology}, keywords = {filamin, integrin, migration}, month = {December}, number = {12}, pages = {1060--1068}, posted-at = {2009-10-29 13:33:51}, priority = {2}, title = {Increased filamin binding to beta-integrin cytoplasmic domains inhibits cell migration.}, url = {http://dx.doi.org/10.1038/ncb1201-1060}, volume = {3}, year = {2001} }

TY - JOUR ID - citeulike:6032131 L3 - citeulike-article-id:6032131 N2 - Multicellular animal development depends on integrins. These adhesion receptors link to the actin cytoskeleton, transmitting biochemical signals and force during cell migration and interactions with the extracellular matrix. Many integrin-cytoskeleton connections are formed by filamins and talin. The beta7 integrin tail binds strongly to filamin and supports less migration, fibronectin matrix assembly and focal adhesion formation than either the beta1D tail, which binds strongly to talin, or the beta1A tail, which binds modestly to both filamin and talin. To probe the role of filamin binding, we mapped the filamin-binding site of integrin tails and identified amino acid substitutions that led to selective loss of filamin binding to the beta7 tail and gain of filamin binding to the beta1A tail. These changes affected cell migration and membrane protrusions but not fibronectin matrix assembly or focal adhesion formation. Thus, tight filamin binding restricts integrin-dependent cell migration by inhibiting transient membrane protrusion and cell polarization. IS - 12 JF - Nature cell biology SN - 1465-7392 EP - 1068 TI - Increased filamin binding to beta-integrin cytoplasmic domains inhibits cell migration. VL - 3 SP - 1060 KW - filamin KW - integrin KW - migration AU - Calderwood, DA AU - Huttenlocher, A AU - Kiosses, WB AU - Rose, DM AU - Woodside, DG AU - Schwartz, MA AU - Ginsberg, MH PY - 2001/12// UR - http://dx.doi.org/10.1038/ncb1201-1060 ER -