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Vol. 11, Issue 2, 579-592, February 2000
Department of Anatomy and Structural Biology, Albert Einstein
College of Medicine, Bronx, New York 10461
The plasma membrane ATPase, encoded by PMA1, is
delivered to the cell surface via the secretory pathway. Previously, we
characterized a temperature-sensitive pma1 mutant in
which newly synthesized Pma1-7 is not delivered to the plasma membrane
but is mislocalized instead to the vacuole at 37°C. Several
vps mutants, which are defective in vacuolar protein
sorting, suppress targeting-defective pma1 by allowing
mutant Pma1 to move once again to the plasma membrane. In this study,
we have analyzed trafficking in the endosomal system by monitoring the
movement of Pma1-7 in vps36, vps1, and vps8 mutants. Upon induction of expression, mutant Pma1
accumulates in the prevacuolar compartment in vps36
cells. After chase, a fraction of newly synthesized Pma1-7 is delivered
to the plasma membrane. In both vps1 and
vps8 cells, newly synthesized mutant Pma1 appears in
small punctate structures before arrival at the cell surface.
Nevertheless, biosynthetic membrane traffic appears to follow different
routes in vps8 and vps1: the vacuolar
protein-sorting receptor Vps10p is stable in vps8 but
not in vps1. Furthermore, a defect in endocytic delivery
to the vacuole was revealed in vps8 (and
vps36) but not vps1 by endocytosis of the
bulk membrane marker FM 4-64. Moreover, in vps8 cells,
there is defective down-regulation from the cell surface of the mating
receptor Ste3, consistent with persistent receptor recycling from an
endosomal compartment to the plasma membrane. These data support a
model in which mutant Pma1 is diverted from the Golgi to the surface in
vps1 cells. We hypothesize that in vps8
and vps36, in contrast to vps1, mutant Pma1 moves to the surface via endosomal intermediates, implicating an
endosome-to-surface traffic pathway.
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