4rey: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:
'''Unreleased structure'''
==Crystal Structure of the GRASP65-GM130 C-terminal peptide complex==
<StructureSection load='4rey' size='340' side='right' caption='[[4rey]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rey]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4REY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4REY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rey OCA], [http://pdbe.org/4rey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rey RCSB], [http://www.ebi.ac.uk/pdbsum/4rey PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GORS1_HUMAN GORS1_HUMAN]] Stacking factor involved in the postmitotic assembly of Golgi stacks from mitotic Golgi fragments. Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (PubMed:16489344).[UniProtKB:O35254]<ref>PMID:16489344</ref>  [[http://www.uniprot.org/uniprot/GOGA2_HUMAN GOGA2_HUMAN]] Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane. Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (By similarity). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (PubMed:19242490, PubMed:26165940). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (PubMed:18045989, PubMed:19109421). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (PubMed:16489344, PubMed:17314401).[UniProtKB:Q62839][UniProtKB:Q921M4]<ref>PMID:16489344</ref> <ref>PMID:17314401</ref> <ref>PMID:18045989</ref> <ref>PMID:19109421</ref> <ref>PMID:19242490</ref> <ref>PMID:26165940</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GM130 and GRASP65 are Golgi peripheral membrane proteins that play a key role in Golgi stacking and vesicle tethering. However, the molecular details of their interaction and their structural role as a functional unit remain unclear. Here, we present the crystal structure of the PDZ domains of GRASP65 in complex with the GM130 C-terminal peptide at 1.96-A resolution. In contrast to previous findings proposing that GM130 interacts with GRASP65 at the PDZ2 domain only, our crystal structure of the complex indicates that GM130 binds to GRASP65 at two distinct sites concurrently and that both the PDZ1 and PDZ2 domains of GRASP65 participate in this molecular interaction. Mutagenesis experiments support these structural observations and demonstrate that they are required for GRASP65-GM130 association.


The entry 4rey is ON HOLD  until Paper Publication
Structural Basis for the Interaction between the Golgi Reassembly-stacking Protein GRASP65 and the Golgi Matrix Protein GM130.,Hu F, Shi X, Li B, Huang X, Morelli X, Shi N J Biol Chem. 2015 Oct 30;290(44):26373-82. doi: 10.1074/jbc.M115.657940. Epub, 2015 Sep 11. PMID:26363069<ref>PMID:26363069</ref>


Authors: Shi, N., Hu, F., Li, B.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal Structure of the GRASP complex
<div class="pdbe-citations 4rey" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hu, F]]
[[Category: Hu, F]]
[[Category: Li, B]]
[[Category: Shi, N]]
[[Category: Shi, N]]
[[Category: Li, B]]
[[Category: Membrane protein]]
[[Category: Pdz fold six-stranded anti parallel-barrel capped by two-helice]]
[[Category: Protein interaction]]

Revision as of 00:17, 1 December 2015

Crystal Structure of the GRASP65-GM130 C-terminal peptide complexCrystal Structure of the GRASP65-GM130 C-terminal peptide complex

Structural highlights

4rey is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[GORS1_HUMAN] Stacking factor involved in the postmitotic assembly of Golgi stacks from mitotic Golgi fragments. Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (PubMed:16489344).[UniProtKB:O35254][1] [GOGA2_HUMAN] Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane. Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (By similarity). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (PubMed:19242490, PubMed:26165940). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (PubMed:18045989, PubMed:19109421). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (PubMed:16489344, PubMed:17314401).[UniProtKB:Q62839][UniProtKB:Q921M4][2] [3] [4] [5] [6] [7]

Publication Abstract from PubMed

GM130 and GRASP65 are Golgi peripheral membrane proteins that play a key role in Golgi stacking and vesicle tethering. However, the molecular details of their interaction and their structural role as a functional unit remain unclear. Here, we present the crystal structure of the PDZ domains of GRASP65 in complex with the GM130 C-terminal peptide at 1.96-A resolution. In contrast to previous findings proposing that GM130 interacts with GRASP65 at the PDZ2 domain only, our crystal structure of the complex indicates that GM130 binds to GRASP65 at two distinct sites concurrently and that both the PDZ1 and PDZ2 domains of GRASP65 participate in this molecular interaction. Mutagenesis experiments support these structural observations and demonstrate that they are required for GRASP65-GM130 association.

Structural Basis for the Interaction between the Golgi Reassembly-stacking Protein GRASP65 and the Golgi Matrix Protein GM130.,Hu F, Shi X, Li B, Huang X, Morelli X, Shi N J Biol Chem. 2015 Oct 30;290(44):26373-82. doi: 10.1074/jbc.M115.657940. Epub, 2015 Sep 11. PMID:26363069[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Puthenveedu MA, Bachert C, Puri S, Lanni F, Linstedt AD. GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat Cell Biol. 2006 Mar;8(3):238-48. Epub 2006 Feb 19. PMID:16489344 doi:http://dx.doi.org/10.1038/ncb1366
  2. ↑ Puthenveedu MA, Bachert C, Puri S, Lanni F, Linstedt AD. GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat Cell Biol. 2006 Mar;8(3):238-48. Epub 2006 Feb 19. PMID:16489344 doi:http://dx.doi.org/10.1038/ncb1366
  3. ↑ Marra P, Salvatore L, Mironov A Jr, Di Campli A, Di Tullio G, Trucco A, Beznoussenko G, Mironov A, De Matteis MA. The biogenesis of the Golgi ribbon: the roles of membrane input from the ER and of GM130. Mol Biol Cell. 2007 May;18(5):1595-608. Epub 2007 Feb 21. PMID:17314401 doi:http://dx.doi.org/10.1091/mbc.E06-10-0886
  4. ↑ Kodani A, Sutterlin C. The Golgi protein GM130 regulates centrosome morphology and function. Mol Biol Cell. 2008 Feb;19(2):745-53. Epub 2007 Nov 28. PMID:18045989 doi:http://dx.doi.org/10.1091/mbc.E07-08-0847
  5. ↑ Kodani A, Kristensen I, Huang L, Sutterlin C. GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization. Mol Biol Cell. 2009 Feb;20(4):1192-200. doi: 10.1091/mbc.E08-08-0834. Epub 2008, Dec 24. PMID:19109421 doi:http://dx.doi.org/10.1091/mbc.E08-08-0834
  6. ↑ Rivero S, Cardenas J, Bornens M, Rios RM. Microtubule nucleation at the cis-side of the Golgi apparatus requires AKAP450 and GM130. EMBO J. 2009 Apr 22;28(8):1016-28. doi: 10.1038/emboj.2009.47. Epub 2009 Feb 26. PMID:19242490 doi:http://dx.doi.org/10.1038/emboj.2009.47
  7. ↑ Wei JH, Zhang ZC, Wynn RM, Seemann J. GM130 Regulates Golgi-Derived Spindle Assembly by Activating TPX2 and Capturing Microtubules. Cell. 2015 Jul 16;162(2):287-99. doi: 10.1016/j.cell.2015.06.014. Epub 2015 Jul, 9. PMID:26165940 doi:http://dx.doi.org/10.1016/j.cell.2015.06.014
  8. ↑ Hu F, Shi X, Li B, Huang X, Morelli X, Shi N. Structural Basis for the Interaction between the Golgi Reassembly-stacking Protein GRASP65 and the Golgi Matrix Protein GM130. J Biol Chem. 2015 Oct 30;290(44):26373-82. doi: 10.1074/jbc.M115.657940. Epub, 2015 Sep 11. PMID:26363069 doi:http://dx.doi.org/10.1074/jbc.M115.657940

4rey, resolution 1.96Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4rey&oldid=2499546"