Leupaxin binds to PEST domain tyrosine phosphatase PEP |
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Authors: | Watanabe Noriyuki Amano Natsuko Ishizuka Hajime Mashima Keisuke |
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Institution: | Department of Life Science and Frontier Project "Life's Adaptation Strategies to Environmental Changes," Rikkyo (St Paul's) University, Nishi-Ikebukuro, Toshima-ku, Tokyo, Japan. |
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Abstract: | PEST domain tyrosine phosphatase (PEP) is an intracellular protein tyrosine phosphatase and characterized by PEST motifs and proline-rich domains in the carboxyl terminal half. PEP is primarily expressed in hematopoietic cells, and together with PEP-binding Csk, may act as a negative regulator of antigen receptor signaling in lymphocytes. Here, we show the binding capability of PEP for leupaxin, which is preferentially expressed in hematopoietic cells and a comparatively new member of the paxillin family characterized by two protein-protein interaction modules, LIM domains and LD motifs. These results suggested that leupaxin might participate in the regulation of the signaling cascade through the binding to PEP in lymphocytes. |
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