4kfv
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4kfv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KFV FirstGlance]. <br> | <table><tr><td colspan='2'>[[4kfv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KFV FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfv OCA], [https://pdbe.org/4kfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kfv RCSB], [https://www.ebi.ac.uk/pdbsum/4kfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kfv ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfv OCA], [https://pdbe.org/4kfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kfv RCSB], [https://www.ebi.ac.uk/pdbsum/4kfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kfv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GORS1_RAT GORS1_RAT] Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (By similarity). However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis (PubMed:12839990, PubMed:23940043, PubMed:9346242). Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis (PubMed:11815631, PubMed:12015985). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity).[UniProtKB:Q91X51][UniProtKB:Q9BQQ3]<ref>PMID:11815631</ref> <ref>PMID:12015985</ref> <ref>PMID:12839990</ref> <ref>PMID:23940043</ref> <ref>PMID:9346242</ref> | [https://www.uniprot.org/uniprot/GORS1_RAT GORS1_RAT] Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (By similarity). However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis (PubMed:12839990, PubMed:23940043, PubMed:9346242). Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis (PubMed:11815631, PubMed:12015985). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity).[UniProtKB:Q91X51][UniProtKB:Q9BQQ3]<ref>PMID:11815631</ref> <ref>PMID:12015985</ref> <ref>PMID:12839990</ref> <ref>PMID:23940043</ref> <ref>PMID:9346242</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The stacking of Golgi cisternae involves GRASP65 and GRASP55. The oligomerization of the N-terminal GRASP domain of these proteins, which consists of two tandem PDZ domains, is required to tether the Golgi membranes. However, the molecular basis for GRASP assembly is unclear. Here, we determined the crystal structures of the GRASP domain of GRASP65 and GRASP55. The structures reveal similar homotypic interactions: the GRASP domain forms a dimer in which the peptide-binding pockets of the two neighboring PDZ2 domains face each other, and the dimers are further connected by the C-terminal tail of one GRASP domain inserting into the binding pocket of the PDZ1 domain in another dimer. Biochemical analysis suggests that both types of contacts are relatively weak but are needed in combination for GRASP-mediated Golgi stacking. Our results unveil a novel mode of membrane tethering by GRASP proteins and provide insight into the mechanism of Golgi stacking. | ||
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| - | Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins.,Feng Y, Yu W, Li X, Lin S, Zhou Y, Hu J, Liu X J Biol Chem. 2013 Sep 27;288(39):28418-27. doi: 10.1074/jbc.M113.478024. Epub, 2013 Aug 12. PMID:23940043<ref>PMID:23940043</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4kfv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structural insight into Golgi membrane stacking by GRASP65 and GRASP55
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