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Volume 272, Number 11, Issue of March 14, 1997 pp. 7437-7444
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Monocyte Cells and Cancer Cells Express Novel Paxillin Isoforms with Different Binding Properties to Focal Adhesion Proteins

(Received for publication, May 30, 1996, and in revised form, November 18, 1996)

Yuichi Mazaki , Shigeru Hashimoto ^§ and Hisataka Sabe

From the  Institute for Virus Research, Kyoto University, Kyoto 606, Japan,  Precursory Research for Embryonic Science and Technology, Japan Science and Technology Corporation, Kyoto 619-02, Japan and ^§ Center for Molecular and Cellular Biology, Osaka University, Suita, Osaka 565, Japan

The versatility of integrin functions is mediated by engagement of a number of proteins that assemble with integrins. Among them, paxillin is one of the important molecules interacting with a variety of signaling molecules and cytoskeletal building blocks. We report here that paxillin is not a single molecule with a unique physiological property. We identified two human paxillin isoforms,  and . These isoforms have distinct amino acid insertions; each consists of a distinct exon, at the same site of previously reported paxillin (paxillin ). Several proteins were co-precipitated with paxillin, and we found that  bound to focal adhesion kinase but weakly to vinculin, and  bound to vinculin but only weakly to focal adhesion kinase, although both bound equally to talin. No additional proteins were found to bind to  and  over those binding to . Unlike the  isoform,  and  mRNAs were not detected in normal tissues, but several cancer cells expressed both  and  proteins simultaneously. All three isoform proteins were expressed in promonocytic cells with ratios comparable with each other, and the expression patterns were altered during differentiation of floating promonocytic cells into adherent macrophage-like cells. Therefore, each isoform of paxillin exhibits distinct expression and different biochemical as well as physiological properties and thereby appears to act as a distinct module involved in different functions of integrins.

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