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Published online 4 September 2000. doi:10.1083/jcb.150.5.1113
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© The Rockefeller University Press, 0021-9525/2000//1113 $5.00
The Journal of Cell Biology, Volume 150, Number 5, , 2000 1113-1124

Original Article

Annexins in Cell Membrane Dynamics

: Ca2+-Regulated Association of Lipid Microdomains



Eduard B. Babiychuka,b and Annette Draegera

a Institute of Anatomy, University of Bern, 3012 Bern, Switzerland
b Institute of Physiology, Kiev University, 252031 Kiev, Ukraine
Department of Cell Biology, Institute of Anatomy, University of Bern, Bühlstrasse 26, CH - 3012 Bern, Switzerland.41-31-631-38-0741-31-631-46-25

draeger{at}ana.unibe.ch

The sarcolemma of smooth muscle cells is composed of alternating stiff actin-binding, and flexible caveolar domains. In addition to these stable macrodomains, the plasma membrane contains dynamic glycosphingolipid- and cholesterol-enriched microdomains, which act as sorting posts for specific proteins and are involved in membrane trafficking and signal transduction. We demonstrate that these lipid rafts are neither periodically organized nor exclusively confined to the actin attachment sites or caveolar regions. Changes in the Ca2+ concentration that are affected during smooth muscle contraction lead to important structural rearrangements within the sarcolemma, which can be attributed to members of the annexin protein family. We show that the associations of annexins II, V, and VI with smooth muscle microsomal membranes exhibit a high degree of Ca2+ sensitivity, and that the extraction of annexins II and VI by detergent is prevented by elevated Ca2+ concentrations. Annexin VI participates in the formation of a reversible, membrane–cytoskeleton complex (Babiychuk, E.B., R.J. Palstra, J. Schaller, U. Kämpfer, and A. Draeger. 1999. J. Biol. Chem. 274:35191–35195). Annexin II promotes the Ca2+-dependent association of lipid raft microdomains, whereas annexin V interacts with glycerophospholipid microcompartments. These interactions bring about a new configuration of membrane-bound constituents, with potentially important consequences for signaling events and Ca2+ flux.

Key Words: DIGs • smooth muscle • rafts • caveolae • contraction

© 2000 The Rockefeller University Press

Abbreviation used in this paper: DIG, detergent-insoluble glycosphingolipid.


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