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 reqiured for autophagy. These advances illustrate how the TRAPP complexes link Ypt1 and RAB1 activation to distinct membrane-tethering events.
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Acknowledgements
Salary support for J.B. is provided by US National Institutes of Health (NIH) grant R01 GM41223. Salary support for S.F.-N., and D.B. is provided by the Howard Hughes Medical Institute. Salary support for K.R. is provided by NIH grant R01 GM80616.
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Barrowman, J., Bhandari, D., Reinisch, K. et al. TRAPP complexes in membrane traffic: convergence through a common Rab. Nat Rev Mol Cell Biol 11, 759–763 (2010). https://doi.org/10.1038/nrm2999
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DOI: https://doi.org/10.1038/nrm2999
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