Format

Send to

Choose Destination
See comment in PubMed Commons below
Dev Cell. 2011 Jan 18;20(1):47-59. doi: 10.1016/j.devcel.2010.11.006.

PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast.

Author information

1
Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.

Abstract

Cell polarity involves transport of specific membranes and macromolecules at the right time to the right place. In budding yeast, secretory vesicles are transported by the myosin-V Myo2p to sites of cell growth. We show that phosphatidylinositol 4-phosphate (PI4P) is present in late secretory compartments and is critical for their association with, and transport by, Myo2p. Further, the trans-Golgi network Rab Ypt31/32p and secretory vesicle Rab Sec4p each bind directly, but distinctly, to Myo2p, and these interactions are also required for secretory compartment transport. Enhancing the interaction of Myo2p with PI4P bypasses the requirement for interaction with Ypt31/32p and Sec4p. Together with additional genetic data, the results indicate that Rab proteins and PI4P collaborate in the association of secretory compartments with Myo2p. Thus, we show that a coincidence detection mechanism coordinates inputs from PI4P and the appropriate Rab for secretory compartment transport.

PMID:
21238924
PMCID:
PMC3025538
DOI:
10.1016/j.devcel.2010.11.006
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center