Vesicle Transport: Springing the TRAPP
نویسنده
چکیده
When a coated transport vesicle docks with its target membrane, the coat proteins and docking machinery must be released before the membranes can fuse. A recent paper shows how this disassembly is triggered at precisely the right time.
منابع مشابه
TRAPP Complexes in Secretion and Autophagy
TRAPP is a highly conserved modular multi-subunit protein complex. Originally identified as a "transport protein particle" with a role in endoplasmic reticulum-to-Golgi transport, its multiple subunits and their conservation from yeast to humans were characterized in the late 1990s. TRAPP attracted attention when it was shown to act as a Ypt/Rab GTPase nucleotide exchanger, GEF, in the 2000s. C...
متن کاملThe structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex.
The TRAPP (transport protein particle) complexes are tethering complexes that have an important role at the different steps of vesicle transport. Recently, the crystal structures of the TRAPP subunits SEDL and BET3 have been determined, and we present here the 1.7 Angstroms crystal structure of human TPC6, a third TRAPP subunit. The protein adopts an alpha/beta-plait topology and forms a dimer....
متن کاملTRAPP stably associates with the Golgi and is required for vesicle docking.
Bet3p, a component of a large novel complex called TRAPP, acts upstream of endoplasmic reticulum (ER)-Golgi SNAREs. Unlike the SNAREs, which reside on multiple compartments, Bet3p is localized exclusively to Golgi membranes. While other proteins recycle from the Golgi to the ER, Bet3p and other TRAPP subunits remain associated with this membrane under conditions that block anterograde traffic. ...
متن کاملTRAPPC9 Mediates the Interaction between p150Glued and COPII Vesicles at the Target Membrane
BACKGROUND The transport of endoplasmic reticulum (ER)-derived COPII vesicles toward the ER-Golgi intermediate compartment (ERGIC) requires cytoplasmic dynein and is dependent on microtubules. p150(Glued), a subunit of dynactin, has been implicated in the transport of COPII vesicles via its interaction with COPII coat components Sec23 and Sec24. However, whether and how COPII vesicle tether, TR...
متن کاملTRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion.
We previously identified BET3 by its genetic interactions with BET1, a gene whose SNARE-like product acts in endoplasmic reticulum (ER)-to-Golgi transport. To gain insight into the function of Bet3p, we added three c-myc tags to its C-terminus and immunopurified this protein from a clarified detergent extract. Here we report that Bet3p is a member of a large complex ( approximately 800 kDa) tha...
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عنوان ژورنال:
- Current Biology
دوره 21 شماره
صفحات -
تاریخ انتشار 2011