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SHPS‐1, a multifunctional transmembrane glycoprotein
Author(s) -
Oshima Kumi,
Ruhul Amin A.R.M,
Suzuki Atsushi,
Hamaguchi Michinari,
Matsuda Satoru
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02703-5
Subject(s) - microbiology and biotechnology , protein tyrosine phosphatase , proto oncogene tyrosine protein kinase src , biology , cd47 , transmembrane protein , signal transducing adaptor protein , sh3 domain , signal transduction , receptor , biochemistry , phagocytosis
Src homology 2 (SH2) domain‐containing protein tyrosine phosphatase substrate 1 (SHPS‐1) is a member of the signal regulatory protein (SIRP) family. The amino‐terminal immunoglobulin‐like domain of SHPS‐1 is necessary for interaction with CD47, a ligand for SHPS‐1, which plays an important role in cell–cell interaction. The intracellular region of SHPS‐1, on the other hand, may act as a scaffold protein, binding to various adapter proteins. Interestingly, increasing evidence has shown that SHPS‐1 is involved in various biological phenomena, including suppression of anchorage‐independent cell growth, negative regulation of immune cells, self‐recognition of red blood cells, mediation of macrophage multinucleation, skeletal muscle differentiation, entrainment of circadian clock, neuronal survival and synaptogenesis. Recent progress has been made in attributing these novel exciting functions. Here we discuss how this interesting molecule works and consider its true role in biology.