The paxillin family of LIM domain-containing proteins includes paxillin, Hic-5, and leupaxin. Similar to other family members, leupaxin is composed of multiple functional modules, including leucine and aspartate motifs and LIM domains. These domains suggest that leupaxin is a molecular adaptor that may be important for integrin-mediated cell signaling. Leupaxin was identified in leukocytes, and has been shown to be expressed in non-hematopoietic lineage cells, including vascular smooth muscle cells and certain cancer cells. In prostate cancer cells, leupaxin expression intensity is directly linked to cancer progression. Leupaxin localizes to the podosomal signaling complex in murine osteoclasts where it may be important for rearrangement of cytoskeletal components. The function of leupaxin in regulating the cytoskeleton may involve protein-protein interactions between leupaxin and focal adhesion proteins, such as Pyk2, FAK, Src, Lyn, and PTP-PEST.
Tanaka, T. et al. (2010) Cancer Sci. 101:363.
Sundberg-Smith, L.J. et al. (2008) Circ Res. 102(12):1502.
*For more information, see UniProt Accession O60711
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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