Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?
The spatial segregation of the plasma membrane plays a prominent role in distinguishing and sorting a large number of signals a cell receives simultaneously. The plasma membrane comprises regions known as lipid rafts, which serve as signal-transduction hubs and platforms for sorting membrane-associated proteins. Ca(2+)-binding proteins of the annexin family have been ascribed a role in the regulation of raft dynamics. Glycosylphosphatidylinositol-anchored 5'-nucleotidase is an extracellular, raft-associated enzyme responsible for conversion of extracellular ATP into adenosine. Our results point to a regulation of ecto-5'-nucleotidase activity by Ca(2+)-dependent, annexin-mediated stabilization of membrane rafts.
Babiychuk
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EB
Department of Cell Biology, Institute of Anatomy, University of Bern, Switzerland.
Draeger
A
A
D015720:5'-Nucleotidase / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D017306:Annexin A2 / Q000737:chemistry / Q000502:physiology*; D002118:Calcium / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D021962:Membrane Microdomains / Q000201:enzymology*; D032389:Myocytes, Smooth Muscle / Q000201:enzymology
D017306:Annexin A2; D015720:5'-Nucleotidase; D002118:Calcium