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Retromer recruitment

Phosphoinositide 3-kinases (PI3Ks) play important roles in membrane trafficking: they generate the phospholipid PtdIns(3)P, which can recruit effector proteins containing FYVE or PX domains to intracellular membranes. The yeast PI3K Vps34p forms part of a multiprotein assembly termed complex II that contains three other proteins — Vps15p, Vps30p and Vps38p — and is required for maturation of the cargo molecule carboxypeptidase Y (CPY). Scott Emr and co-workers have studied the role of this complex by analysing membrane trafficking in VPS30 and VPS38 mutants (see p. 3889). They find that the mutants exhibit defective sorting of CPY and another cargo molecule, Kex2p. They also observe mislocalization of two other proteins — Vps5p and Vps17p — PX-domain proteins that form part of the retromer complex required for endosome-to-Golgi transport. Significantly, a vacuolar PX-domain protein, Vam7p, does not mislocalize in these cells, which indicates that the effect is specific. The authors go on to show that Vps5p and Vps17p bind specifically to PtdIns(3)P in vitro and in vivo, concluding that complex II directs synthesis of an endosomal pool of PtdIns(3)P that recruits the retromer complex to ensure efficient endosome-to-Golgi transport.

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Related articles in JCS:

Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase

Patricie Burda, Steven M. Padilla, Srimonti Sarkar, and Scott D. Emr
JCS 2002 115: 3889-3900. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?