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Coat complexes are important for cargo selection and vesicle formation. Recent evidence suggests that they may also be involved in vesicle targeting. Tethering factors, which form an initial bridge between vesicles and the target membrane, may bind to coat complexes. In this review, we ask whether these coat/tether interactions share some common mechanisms, or whether they are special adaptations to the needs of very specific transport steps. We compare recent findings in two multisubunit tethering complexes, the Dsl1 complex and the HOPS complex, and put them into context with the TRAPP I complex as a prominent example for coat/tether interactions. We explore where coat/tether interactions are found, compare their function and structure, and comment on a possible evolution from a common ancestor of coats and tethers.
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http://dx.doi.org/10.3389/fcell.2016.00044 | DOI Listing |
Front Cell Dev Biol
September 2016
Neurobiology, Max Planck Institute for Biophysical Chemistry Göttingen, Germany.
[This corrects the article on p. 44 in vol. 4, PMID: 27243008.
View Article and Find Full Text PDFFront Cell Dev Biol
May 2016
Neurobiology, Max Planck Institute for Biophysical Chemistry Göttingen, Germany.
Coat complexes are important for cargo selection and vesicle formation. Recent evidence suggests that they may also be involved in vesicle targeting. Tethering factors, which form an initial bridge between vesicles and the target membrane, may bind to coat complexes.
View Article and Find Full Text PDFMol Biol Cell
July 2008
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213, USA.
Biogenesis of the Golgi apparatus is likely mediated by the COPI vesicle coat complex, but the mechanism is poorly understood. Modeling of the COPI subunit betaCOP based on the clathrin adaptor AP2 suggested that the betaCOP C terminus forms an appendage domain with a conserved FW binding pocket motif. On gene replacement after knockdown, versions of betaCOP with a mutated FW motif or flanking basic residues yielded a defect in Golgi organization reminiscent of that occurring in the absence of the vesicle tether p115.
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