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Leupaxin binds to PEST domain tyrosine phosphatase PEP
Authors:Watanabe Noriyuki  Amano Natsuko  Ishizuka Hajime  Mashima Keisuke
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.
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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