SHPS-1, a multifunctional transmembrane glycoprotein

FEBS Lett. 2002 May 22;519(1-3):1-7. doi: 10.1016/s0014-5793(02)02703-5.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antigens, CD / metabolism
  • Antigens, Differentiation*
  • CD47 Antigen
  • Carrier Proteins / metabolism
  • Cell Communication / physiology
  • Cell Division / physiology
  • Humans
  • Membrane Glycoproteins / metabolism*
  • Neural Cell Adhesion Molecule L1*
  • Neural Cell Adhesion Molecules / metabolism*
  • Receptors, Immunologic / metabolism*
  • Signal Transduction / physiology*

Substances

  • Antigens, CD
  • Antigens, Differentiation
  • CD47 Antigen
  • CD47 protein, human
  • Carrier Proteins
  • Membrane Glycoproteins
  • Neural Cell Adhesion Molecule L1
  • Neural Cell Adhesion Molecules
  • Receptors, Immunologic
  • SIRPA protein, human