Abstract
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 required for autophagy. These advances illustrate how the TRAPP complexes link Ypt1 and RAB1 activation to distinct membrane-tethering events.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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Endoplasmic Reticulum / metabolism
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Golgi Apparatus / metabolism
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Guanine Nucleotide Exchange Factors / genetics
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Guanine Nucleotide Exchange Factors / metabolism*
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Humans
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Intercellular Signaling Peptides and Proteins
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Models, Biological
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Mutation
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Vesicular Transport Proteins / genetics
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Vesicular Transport Proteins / metabolism*
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rab1 GTP-Binding Proteins / metabolism*
Substances
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Carrier Proteins
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Guanine Nucleotide Exchange Factors
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Intercellular Signaling Peptides and Proteins
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TRAPPC9 protein, human
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Vesicular Transport Proteins
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transport protein particle, TRAPP
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rab1 GTP-Binding Proteins