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. 2001 Jan 8;152(1):181–196. doi: 10.1083/jcb.152.1.181

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© 2001 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Cbl associates with Pyk2 in a Src-dependent manner, and becomes tyrosine phosphorylated by Src in a reaction that also requires the presence of Pyk2. Immunocytochemistry showing Pyk2 and Cbl colocalization in Src⁺ authentic osteoclasts. Micrographs represent individual channels (red, Pyk2; green, Cbl) and a merging of the two channels. Pyk2 was immunoprecipitated from Src⁺ and Src⁻ OCLs. Immune complexes were Western blotted for Cbl (top left), and then the membranes were stripped and reprobed with Pyk2 antibodies (bottom left) Total cell lysates (TCL) were also electrophoresed along with the immunoprecipitates. Reciprocal immunoprecipitation and blotting was performed using Cbl antibodies for immunoprecipitation and Pyk2 antibodies for blotting (top right). The membrane was stripped and reprobed with Cbl antibodies (bottom right).