Abstract

Zyxin is a component of adhesion plaques that has been suggested to perform regulatory functions at these specialized regions of the plasma membrane. Here we describe the isolation and characterization of cDNAs encoding human and mouse zyxin. Both the human and mouse zyxin proteins display a collection of proline-rich sequences as well as three copies of the LIM domain, a zinc finger domain found in many signaling molecules. The human zyxin protein is closely related in sequence to proteins implicated in benign tumorigenesis and steroid receptor binding. Antibodies raised against human zyxin recognize an 84-kDa protein by Western immunoblot analysis. The protein is localized at focal contacts in adherent erythroleukemia cells. By Northern analysis, we show that zyxin is widely expressed in human tissues. The zyxin gene maps to human chromosome 7q32-q36.

Keywords

LIM domainZinc fingerBiologyFocal adhesionCell biologyProtein subcellular localization predictionSemaphorinRING finger domainGeneReceptorGeneticsSignal transductionTranscription factor

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Publication Info

Year
1996
Type
article
Volume
271
Issue
49
Pages
31470-31478
Citations
113
Access
Closed

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Teresita Macalma, Jürgen Otte, Mary E. Hensler et al. (1996). Molecular Characterization of Human Zyxin. Journal of Biological Chemistry , 271 (49) , 31470-31478. https://doi.org/10.1074/jbc.271.49.31470

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DOI
10.1074/jbc.271.49.31470