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Vol. 12, Issue 12, 4129-4138, December 2001
and
*Max Plank Institute for Molecular Cell Biology and Genetics, 01307 Dresden, Germany; and Correct sorting of proteins is essential to generate and maintain
the identity and function of the different cellular compartments. In
this study we demonstrate the role of lipid rafts in biosynthetic delivery of Pma1p, the major plasma membrane proton ATPase, to the cell
surface. Disruption of rafts led to mistargeting of Pma1p to the
vacuole. Conversely, Pma1-7, an ATPase mutant that is mistargeted to
the vacuole, was shown to exhibit impaired raft association. One of the
previously identified suppressors, multicopy AST1, not
only restored surface delivery but also raft association of Pma1-7.
Ast1p, which is a peripheral membrane protein, was found to directly
interact with Pma1p inducing its clustering into a SDS/Triton
X100-resistant oligomer. We suggest that clustering facilitates
partition of Pma1p into rafts and transport to the cell surface.
Department of Anatomy and
Structural Biology, Albert Einstein College of Medicine, Bronx, New
York 10461
Corresponding author. E-mail address:
simons{at}mpi-cbg.de.
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