Annexin II tetramer: structure and function

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276 Citas (Scopus)

Resumen

The annexins are a family of proteins that bind acidic phospholipids in the presence of Ca2+. The interaction of these proteins with biological membranes has led to the suggestion that these proteins may play a role in membrane trafficking events such as exocytosis, endocytosis and cell-cell adhesion. One member of the annexin family, annexin II, has been shown to exist as a monomer, heterodimer or heterotetramer. The ability of annexin II tetramer to bridge secretory granules to plasma membrane has suggested that this protein may play a role in Ca2+-dependent exocytosis. Annexin II tetramer has also been demonstrated on the extracellular face of some metastatic cells where it mediates the binding of certain metastatic cells to normal cells. Annexin II tetramer is a major cellular substrate of protein kinase C and pp60src. Phosphorylation of annexin II tetramer is a negative modulator of protein function.

Idioma originalEnglish
Páginas (desde-hasta)301-322
Número de páginas22
PublicaciónMolecular and Cellular Biochemistry
Volumen149-150
N.º1
DOI
EstadoPublished - ago. 1995
Publicado de forma externa

ASJC Scopus Subject Areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

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Citar esto

Waisman, D. M. (1995). Annexin II tetramer: structure and function. Molecular and Cellular Biochemistry, 149-150(1), 301-322. https://doi.org/10.1007/BF01076592