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PMID: 21550243 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Rabs and the exocyst in ciliogenesis, tubulogenesis and beyond.

Trends in cell biology ·Vol. 21 ·No. 7 ·2011-07-00 ·Pages 383-6

Das A, Guo W

Abstract

The exocyst, an octameric protein complex mediating vesicle tethering at the plasma membrane for exocytosis, is a downstream effector of the Rab proteins Rab8 and Rab11, which are key regulators of membrane trafficking from the trans-Golgi network and recycling endosome to the plasma membrane. Rab11 and Rab8 coordinate their actions via Rabin8, the guanine nucleotide exchange factor of Rab8. A cascade of protein-protein interactions involving the Rabs and the exocyst complex couples the generation of secretory vesicles at donor compartments to their docking and fusion at the plasma membrane. Here, we discuss recent work implicating Rab proteins and the exocyst in primary ciliogenesis and epithelial lumenogenesis. In addition, we discuss early work in the budding yeast Saccharomyces cerevisiae, which provided the initial insight into the molecular mechanisms of polarized exocytosis.

MeSH Terms
Cell Membrane/metabolism Cell Polarity Cilia/metabolism Epithelial Cells/metabolism Exocytosis Humans Saccharomyces cerevisiae/cytology,metabolism rab GTP-Binding Proteins/metabolism
Chemicals
rab GTP-Binding Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Das Amlan
Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Guo Wei
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Article Info
Journal
Trends in cell biology
Abbr.
Trends Cell Biol
ISSN
1879-3088
DOI
10.1016/j.tcb.2011.03.006
Published
2011-07-00
Epub
2011-00-06
Pages
383-6
Language
English
Region
England
NLM ID
9200566
PMCID
PMC3128673
Subset
IM
Grants
NIGMS NIH HHS · R01 GM064690 · United States
NIGMS NIH HHS · R01 GM064690-09 · United States
NIGMS NIH HHS · R01 GM085146 · United States
NIGMS NIH HHS · R01 GM085146-03 · United States
External Links
PubMed source DOI: 10.1016/j.tcb.2011.03.006 PMC Full Text View journal details
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