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doi: 10.1242/10.1242/jcs.00090
Research Article |
Department of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California at San Diego, School of Medicine, La Jolla, CA 92093-0668, USA
* Author for correspondence (e-mail: semr{at}ucsd.edu)
Accepted 2 August 2002
A direct role for phosphoinositides in vesicular trafficking has been
demonstrated by the identification of the yeast VPS34 gene encoding
the phosphatidylinositol 3-kinase responsible for the synthesis of
phosphatidylinositol 3-phosphate (PtdIns3P). Vps34p binds the protein
kinase Vps15p, and it has recently been shown that Vps15p and Vps34p associate
with Vps30p and Vps38p to form a multimeric complex, termed complex II. We
observed that mutations in the VPS30 and VPS38 genes led to
a selective sorting and maturation phenotype of the soluble vacuolar protease
CPY. Localization studies revealed that the CPY receptor Vps10p and the
Golgi-endoprotease Kex2p were mislocalized to vacuolar membranes in strains
deficient for either Vps30p or Vps38p, respectively. Interestingly, we
measured decreased PtdIns3P levels in 
vps30 and
vps38 cells and observed redistribution of Vps5p and Vps17p to
the cytoplasm in these mutants. Vps5p and Vps17p are subunits of the retromer
complex that is required for endosome-to-Golgi retrograde transport. Both
proteins contain the Phox homology (PX) domain, a recently identified
phosphoinositide-binding motif. We demonstrate that the PX domains of Vps5p
and Vps17p specifically bind to PtdIns3P in vitro and in vivo. On the
basis of these and other observations, we propose that the PtdIns 3-kinase
complex II directs the synthesis of a specific endosomal pool of
PtdIns3P, which is required for recruitment/activation of the
retromer complex, thereby ensuring efficient endosome-to-Golgi retrograde
transport.
Key words: Vesicular transport, Endosome-to-Golgi retrograde transport, PX domain, Phosphatidylinositol 3-phosphate, Saccharomyces cerevisiae
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