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TRAPP complexes in membrane traffic: convergence through a common Rab

Journal

NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 11, Issue 11, Pages 759-763

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nrm2999

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Funding

  1. US National Institutes of Health (NIH) [R01 GM41223]
  2. Howard Hughes Medical Institute
  3. NIH [R01 GM80616]

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Transport protein particle (TRAPP; also known as trafficking protein particle), a multimeric guanine nucleotide-exchange factor for the yeast GTPase Ypt1 and its mammalian homologue, RAB1, regulates multiple membrane trafficking pathways. TRAPP complexes exist in three forms, each of which activates Ypt1 or RAB1 through a common core of subunits and regulates complex localization through distinct subunits. Whereas TRAPPI and TRAPPII tether coated vesicles during endoplasmic reticulum to Golgi and intra-Golgi traffic, respectively, TRAPPIII has recently been shown to be reqiured for autophagy. These advances illustrate how the TRAPP complexes link Ypt1 and RAB1 activation to distinct membrane-tethering events.

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