| Structural highlights
3bbp is a 6 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Related: | |
| Gene: | RAB6A, RAB6 (HUMAN), GCC2, KIAA0336, RANBP2L4 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[RAB6A_HUMAN] Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity. [GCC2_HUMAN] Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
GCC185 is a large coiled-coil protein at the trans Golgi network that is required for receipt of transport vesicles inbound from late endosomes and for anchoring noncentrosomal microtubules that emanate from the Golgi. Here, we demonstrate that recruitment of GCC185 to the Golgi is mediated by two Golgi-localized small GTPases of the Rab and Arl families. GCC185 binds Rab6, and mutation of residues needed for Rab binding abolishes Golgi localization. The crystal structure of Rab6 bound to the GCC185 Rab-binding domain reveals that Rab6 recognizes a two-fold symmetric surface on a coiled coil immediately adjacent to a C-terminal GRIP domain. Unexpectedly, Rab6 binding promotes association of Arl1 with the GRIP domain. We present a structure-derived model for dual GTPase membrane attachment that highlights the potential ability of Rab GTPases to reach binding partners at a significant distance from the membrane via their unstructured and membrane-anchored, hypervariable domains.
Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185.,Burguete AS, Fenn TD, Brunger AT, Pfeffer SR Cell. 2008 Jan 25;132(2):286-98. PMID:18243103[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Reddy JV, Burguete AS, Sridevi K, Ganley IG, Nottingham RM, Pfeffer SR. A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling. Mol Biol Cell. 2006 Oct;17(10):4353-63. Epub 2006 Aug 2. PMID:16885419 doi:http://dx.doi.org/10.1091/mbc.E06-02-0153
- ↑ Efimov A, Kharitonov A, Efimova N, Loncarek J, Miller PM, Andreyeva N, Gleeson P, Galjart N, Maia AR, McLeod IX, Yates JR 3rd, Maiato H, Khodjakov A, Akhmanova A, Kaverina I. Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network. Dev Cell. 2007 Jun;12(6):917-30. PMID:17543864 doi:10.1016/j.devcel.2007.04.002
- ↑ Derby MC, Lieu ZZ, Brown D, Stow JL, Goud B, Gleeson PA. The trans-Golgi network golgin, GCC185, is required for endosome-to-Golgi transport and maintenance of Golgi structure. Traffic. 2007 Jun;8(6):758-73. Epub 2007 May 4. PMID:17488291 doi:http://dx.doi.org/10.1111/j.1600-0854.2007.00563.x
- ↑ Burguete AS, Fenn TD, Brunger AT, Pfeffer SR. Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185. Cell. 2008 Jan 25;132(2):286-98. PMID:18243103 doi:10.1016/j.cell.2007.11.048
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