{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T10:51:35Z","timestamp":1761216695711,"version":"3.41.0"},"reference-count":62,"publisher":"Canadian Science Publishing","issue":"5","license":[{"start":{"date-parts":[[2003,10,1]],"date-time":"2003-10-01T00:00:00Z","timestamp":1064966400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochem. Cell Biol."],"published-print":{"date-parts":[[2003,10,1]]},"abstract":"<jats:p> Integrins are found in adhesion structures, which link the extracelullar matrix to cytoskeletal proteins. Here, we attempt to further define the distribution of \u03b2<jats:sub>1<\/jats:sub> integrins in the context of their association with matrix proteins and other cell surface molecules relevant to the endocytic process. We find that \u03b2<jats:sub>1<\/jats:sub> integrins colocalize with fibronectin in fibrillar adhesion structures. A fraction of caveolin is also organized along these adhesion structures. The extracellular matrix protein laminin is not concentrated in these structures. The \u03b1<jats:sub>4<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub> integrin exhibits a distinct distribution from other \u03b2<jats:sub>1<\/jats:sub> integrins after cells have adhered for 1 h to extracellular matrix proteins but is localized in adhesion structures after 24 h of adhesion. There are differences between the fibronectin receptors: \u03b1<jats:sub>5<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub> integrins colocalize with adaptor protein-2 in coated pits, while \u03b1<jats:sub>4<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub> integrins do not. This parallels our earlier observation that of the two laminin receptors, \u03b1<jats:sub>1<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub> and \u03b1<jats:sub>6<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub>, only \u03b1<jats:sub>a<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub> integrins colocalize with adaptor protein-2 in coated pits. Calcium chelation or inhibition of mitogen-activated protein kinase kinase, protein kinase C, or src did not affect localization of \u03b1<jats:sub>1<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub> and \u03b1<jats:sub>5<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub> integrins in coated pits. Likewise, the integrity of coated-pit structures or adhesion structures is not required for integrin and adaptor protein-2 colocalization. This suggests a robust and possibly constitutive interaction between these integrins and coated pits.Key words: adhesion, endocytosis, extracellular matrix, microscopy, confocal, signalling. <\/jats:p>","DOI":"10.1139\/o03-063","type":"journal-article","created":{"date-parts":[[2003,10,28]],"date-time":"2003-10-28T07:14:56Z","timestamp":1067325296000},"page":"335-348","source":"Crossref","is-referenced-by-count":10,"title":["\u03b2<sub>1<\/sub> integrins are distributed in adhesion structures with fibronectin and caveolin and in coated pits"],"prefix":"10.1139","volume":"81","author":[{"given":"Nikhat D","family":"Boyd","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bosco M. 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