GCC185 plays independent roles in Golgi structure maintenance and AP-1–mediated vesicle tethering
نویسندگان
چکیده
منابع مشابه
GCC185 plays independent roles in Golgi structure maintenance and AP-1–mediated vesicle tethering
GCC185 is a long coiled-coil protein localized to the trans-Golgi network (TGN) that functions in maintaining Golgi structure and tethering mannose 6-phosphate receptor (MPR)-containing transport vesicles en route to the Golgi. We report the identification of two distinct domains of GCC185 needed either for Golgi structure maintenance or transport vesicle tethering, demonstrating the independen...
متن کاملMultiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi.
GCC185, a trans-Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose 6-phosphate receptors (MPRs) to the Golgi and for microtubule nucleation at the Golgi via CLASP proteins. GCC185 localizes to the Golgi by cooperative interaction with Rab6 and Arl1 GTPases at adjacent sites near its C terminus. We show here by y...
متن کاملProtein flexibility is required for vesicle tethering at the Golgi
The Golgi is decorated with coiled-coil proteins that may extend long distances to help vesicles find their targets. GCC185 is a trans Golgi-associated protein that captures vesicles inbound from late endosomes. Although predicted to be relatively rigid and highly extended, we show that flexibility in a central region is required for GCC185’s ability to function in a vesicle tethering cycle. Pr...
متن کاملTransport Vesicle Tethering at the Trans Golgi Network: Coiled Coil Proteins in Action
The Golgi complex is decorated with so-called Golgin proteins that share a common feature: a large proportion of their amino acid sequences are predicted to form coiled-coil structures. The possible presence of extensive coiled coils implies that these proteins are highly elongated molecules that can extend a significant distance from the Golgi surface. This property would help them to capture ...
متن کاملARL4A acts with GCC185 to modulate Golgi complex organization.
ADP-ribosylation factor-like protein 4A (ARL4A) is a developmentally regulated member of the ARF/ARL GTPase family. The primary structure of ARL4A is very similar to that of other ARF/ARL molecules, but its function remains unclear. The trans-Golgi network golgin GCC185 is required for maintenance of Golgi structure and distinct endosome-to-Golgi transport. We show here that GCC185 acts as a ne...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2011
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.201104019