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Updated: Aug 18, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
Leupaxin binds to PEST domain tyrosine phosphatase PEP
Noriyuki Watanabe1, Natsuko Amano, Hajime Ishizuka
1Department 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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