{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T05:16:41Z","timestamp":1791350201525,"version":"4.3.1"},"reference-count":28,"publisher":"Springer Science and Business Media LLC","issue":"9","license":[{"start":{"date-parts":[[2007,8,26]],"date-time":"2007-08-26T00:00:00Z","timestamp":1188086400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Cell Biol"],"published-print":{"date-parts":[[2007,9]]},"DOI":"10.1038\/ncb1626","type":"journal-article","created":{"date-parts":[[2007,8,26]],"date-time":"2007-08-26T13:27:51Z","timestamp":1188134871000},"page":"1046-1056","source":"Crossref","is-referenced-by-count":251,"title":["Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2\/3 complex"],"prefix":"10.1038","volume":"9","author":[{"given":"Bryan","family":"Serrels","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan","family":"Serrels","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valerie G.","family":"Brunton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Holt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gordon W.","family":"McLean","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher H.","family":"Gray","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gareth E.","family":"Jones","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Margaret C.","family":"Frame","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2007,8,26]]},"reference":[{"key":"BFncb1626_CR1","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1016\/S0955-0674(97)80152-4","volume":"9","author":"MD Welch","year":"1997","unstructured":"Welch, M. D., Mallavarapu, A., Rosenblatt, J. & Mitchison, T. J. Actin dynamics in vivo. Curr. Opin. Cell Biol. 9, 54\u201361 (1997).","journal-title":"Curr. Opin. Cell Biol."},{"key":"BFncb1626_CR2","doi-asserted-by":"publisher","first-page":"1009","DOI":"10.1083\/jcb.145.5.1009","volume":"145","author":"TM Svitkina","year":"1999","unstructured":"Svitkina, T. M. & Borisy, G. G. Arp2\/3 complex and actin depolymerizing factor\/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145, 1009\u20131026 (1999).","journal-title":"J. Cell Biol."},{"key":"BFncb1626_CR3","doi-asserted-by":"publisher","first-page":"6181","DOI":"10.1073\/pnas.95.11.6181","volume":"95","author":"RD Mullins","year":"1998","unstructured":"Mullins, R. D., Heuser, J. A. & Pollard, T. D. The interaction of Arp2\/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl Acad. Sci. USA 95, 6181\u20136186 (1998).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncb1626_CR4","doi-asserted-by":"publisher","first-page":"1347","DOI":"10.1016\/S0960-9822(98)00015-3","volume":"8","author":"LM Machesky","year":"1998","unstructured":"Machesky, L. M. & Insall, R. H. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2\/3 complex. Curr. Biol. 8, 1347\u20131356 (1998).","journal-title":"Curr. Biol."},{"key":"BFncb1626_CR5","doi-asserted-by":"publisher","first-page":"6932","DOI":"10.1093\/emboj\/17.23.6932","volume":"17","author":"H Miki","year":"1998","unstructured":"Miki, H., Suetsugu, S. & Takenawa, T. WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 17, 6932\u20136941 (1998).","journal-title":"EMBO J."},{"key":"BFncb1626_CR6","doi-asserted-by":"publisher","first-page":"1679","DOI":"10.1126\/science.1066333","volume":"294","author":"RC Robinson","year":"2001","unstructured":"Robinson, R. C. et al. Crystal structure of Arp2\/3 complex. Science 294, 1679\u20131684 (2001).","journal-title":"Science"},{"key":"BFncb1626_CR7","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/S0092-8674(00)80732-1","volume":"97","author":"R Rohatgi","year":"1999","unstructured":"Rohatgi, R. et al. The interaction between N-WASP and the Arp2\/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221\u2013231 (1999).","journal-title":"Cell"},{"key":"BFncb1626_CR8","doi-asserted-by":"publisher","first-page":"242","DOI":"10.1016\/j.cub.2005.12.033","volume":"16","author":"B Butler","year":"2006","unstructured":"Butler, B., Gao, C., Mersich, A. T. & Blystone, S. D. Purified integrin adhesion complexes exhibit actin-polymerization activity. Curr. Biol. 16, 242\u2013251 (2006).","journal-title":"Curr. Biol."},{"key":"BFncb1626_CR9","doi-asserted-by":"publisher","first-page":"881","DOI":"10.1083\/jcb.200206043","volume":"159","author":"KA DeMali","year":"2002","unstructured":"DeMali, K. A., Barlow, C. A. & Burridge, K. Recruitment of the Arp2\/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881\u2013891 (2002).","journal-title":"J. Cell Biol."},{"key":"BFncb1626_CR10","doi-asserted-by":"publisher","first-page":"9161","DOI":"10.1073\/pnas.92.20.9161","volume":"92","author":"JL Coll","year":"1995","unstructured":"Coll, J. L. et al. Targeted disruption of vinculin genes in F9 and embryonic stem cells changes cell morphology, adhesion, and locomotion. Proc. Natl Acad. Sci. USA 92, 9161\u20139165 (1995).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncb1626_CR11","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1242\/dev.125.2.327","volume":"125","author":"W Xu","year":"1998","unstructured":"Xu, W., Baribault, H. & Adamson, E. D. Vinculin knockout results in heart and brain defects during embryonic development. Development 125, 327\u2013337 (1998).","journal-title":"Development"},{"key":"BFncb1626_CR12","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1038\/377539a0","volume":"377","author":"D Ilic","year":"1995","unstructured":"Ilic, D. et al. Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377, 539\u2013544 (1995).","journal-title":"Nature"},{"key":"BFncb1626_CR13","doi-asserted-by":"publisher","first-page":"6906","DOI":"10.1128\/MCB.17.12.6906","volume":"17","author":"A Richardson","year":"1997","unstructured":"Richardson, A., Malik, R. K., Hildebrand, J. D. & Parsons, J. T. Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation. Mol. Cell Biol. 17, 6906\u20136914 (1997).","journal-title":"Mol. Cell Biol."},{"key":"BFncb1626_CR14","doi-asserted-by":"crossref","first-page":"3673","DOI":"10.1242\/jcs.113.20.3673","volume":"113","author":"XD Ren","year":"2000","unstructured":"Ren, X. D. et al. Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 113, 3673\u20133678 (2000).","journal-title":"J. Cell Sci."},{"key":"BFncb1626_CR15","doi-asserted-by":"publisher","first-page":"8113","DOI":"10.1128\/MCB.24.18.8113-8133.2004","volume":"24","author":"MA Westhoff","year":"2004","unstructured":"Westhoff, M. A., Serrels, B., Fincham, V. J., Frame, M. C. & Carragher, N. O. SRC-mediated phosphorylation of focal adhesion kinase couples actin and adhesion dynamics to survival signaling. Mol. Cell Biol. 24, 8113\u20138133 (2004).","journal-title":"Mol. Cell Biol."},{"key":"BFncb1626_CR16","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1016\/S0092-8674(04)00456-8","volume":"117","author":"CL de Hoog","year":"2004","unstructured":"de Hoog, C. L., Foster, L. J. & Mann, M. RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers. Cell 117, 649\u2013662 (2004).","journal-title":"Cell"},{"key":"BFncb1626_CR17","doi-asserted-by":"publisher","first-page":"9565","DOI":"10.1074\/jbc.M310739200","volume":"279","author":"X Wu","year":"2004","unstructured":"Wu, X., Suetsugu, S., Cooper, L. A., Takenawa, T. & Guan, J. L. Focal adhesion kinase regulation of N-WASP subcellular localization and function. J. Biol. Chem. 279, 9565\u20139576 (2004).","journal-title":"J. Biol. Chem."},{"key":"BFncb1626_CR18","doi-asserted-by":"publisher","first-page":"768","DOI":"10.1016\/S0959-440X(02)00396-2","volume":"12","author":"TD Pollard","year":"2002","unstructured":"Pollard, T. D. & Beltzner, C. C. Structure and function of the Arp2\/3 complex. Curr. Opin. Struct. Biol. 12, 768\u2013774 (2002).","journal-title":"Curr. Opin. Struct. Biol."},{"key":"BFncb1626_CR19","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1042\/bj20040176","volume":"380","author":"TH Millard","year":"2004","unstructured":"Millard, T. H., Sharp, S. J. & Machesky, L. M. Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2\/3 complex. Biochem. J. 380, 1\u201317 (2004).","journal-title":"Biochem. J."},{"key":"BFncb1626_CR20","doi-asserted-by":"publisher","first-page":"1177","DOI":"10.1016\/j.cell.2007.05.041","volume":"129","author":"D Lietha","year":"2007","unstructured":"Lietha, D. et al. Structural basis for the autoinhibition of focal adhesion kinase. Cell 129, 1177\u20131187 (2007).","journal-title":"Cell"},{"key":"BFncb1626_CR21","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1083\/jcb.200511093","volume":"173","author":"P Hotulainen","year":"2006","unstructured":"Hotulainen, P. & Lappalainen, P. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 173, 383\u2013394 (2006).","journal-title":"J. Cell Biol."},{"key":"BFncb1626_CR22","doi-asserted-by":"publisher","first-page":"18652","DOI":"10.1074\/jbc.M603508200","volume":"281","author":"F Guo","year":"2006","unstructured":"Guo, F., Debidda, M., Yang, L., Williams, D. A. & Zheng, Y. Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly. J. Biol. Chem. 281, 18652\u201318659 (2006).","journal-title":"J. Biol. Chem."},{"key":"BFncb1626_CR23","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1038\/35074500","volume":"3","author":"R Chen","year":"2001","unstructured":"Chen, R. et al. Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain. Nature Cell Biol. 3, 439\u2013444 (2001).","journal-title":"Nature Cell Biol."},{"key":"BFncb1626_CR24","doi-asserted-by":"publisher","first-page":"5353","DOI":"10.1128\/MCB.24.12.5353-5368.2004","volume":"24","author":"JM Dunty","year":"2004","unstructured":"Dunty, J. M. et al. FERM domain interaction promotes FAK signaling. Mol. Cell Biol. 24, 5353\u20135368 (2004).","journal-title":"Mol. Cell Biol."},{"key":"BFncb1626_CR25","doi-asserted-by":"publisher","first-page":"1299","DOI":"10.1016\/j.bbrc.2005.07.034","volume":"334","author":"RO Jacamo","year":"2005","unstructured":"Jacamo, R. O. & Rozengurt, E. A truncated FAK lacking the FERM domain displays high catalytic activity but retains responsiveness to adhesion-mediated signals. Biochem. Biophys. Res. Commun. 334, 1299\u20131304 (2005).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"BFncb1626_CR26","doi-asserted-by":"publisher","first-page":"8197","DOI":"10.1074\/jbc.M412021200","volume":"280","author":"LA Cohen","year":"2005","unstructured":"Cohen, L. A. & Guan, J. L. Residues within the first subdomain of the FERM-like domain in focal adhesion kinase are important in its regulation. J. Biol. Chem. 280, 8197\u20138207 (2005).","journal-title":"J. Biol. Chem."},{"key":"BFncb1626_CR27","doi-asserted-by":"publisher","first-page":"632","DOI":"10.1038\/ncb829","volume":"4","author":"E Avizienyte","year":"2002","unstructured":"Avizienyte, E. et al. Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling. Nature Cell Biol. 4, 632\u2013638 (2002).","journal-title":"Nature Cell Biol."},{"key":"BFncb1626_CR28","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1186\/1471-2121-4-5","volume":"4","author":"JC Yarrow","year":"2003","unstructured":"Yarrow, J. C., Lechler, T., Li, R. & Mitchison, T. J. Rapid de-localization of actin leading edge components with BDM treatment. BMC Cell Biol. 4, 5 (2003).","journal-title":"BMC Cell Biol."}],"container-title":["Nature Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/ncb1626.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ncb1626","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ncb1626.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T15:30:19Z","timestamp":1684423819000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/ncb1626"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,8,26]]},"references-count":28,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2007,9]]}},"alternative-id":["BFncb1626"],"URL":"https:\/\/doi.org\/10.1038\/ncb1626","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1090893.544244","asserted-by":"object"}]},"ISSN":["1465-7392","1476-4679"],"issn-type":[{"value":"1465-7392","type":"print"},{"value":"1476-4679","type":"electronic"}],"subject":[],"published":{"date-parts":[[2007,8,26]]}}}