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Characterization and ultrastructural localization of annexin VI from mitochondria
D Rainteau1, P Mansuelle, H Rochat
1Département de Biochimie, UFR Biomédicale des Saints-Pères, Université René Descartes, Paris, France.
FEBS Letters
|February 20, 1995
Abstract:
Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca(2+)-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which strongly suggest that annexin VI is closely associated with the cristae in the inner membrane of mitochondria. These findings are consistent with a calcium channel activity of annexin VI in mitochondria.