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5gmj

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Revision as of 06:46, 13 May 2020

Crystal Structure of GRASP55 GRASP domain in complex with JAM-B C-terminus

Structural highlights

5gmj is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5gmi, 5gml
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GORS2_MOUSE] Plays a role in assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after mitotic breakdown. May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA.^[1] [JAM2_MOUSE] May play a role in the processes of lymphocyte homing to secondary lymphoid organs.

Publication Abstract from PubMed

Spermatogenesis is a dynamic process that is regulated by adhesive interactions between germ and Sertoli cells. Germ cells express the Junctional Adhesion Molecule-C (JAM-C, encoded by Jam3), which localizes to germ/Sertoli cell contacts. JAM-C is involved in germ cell polarity and acrosome formation. Using a proteomic approach, we demonstrated that JAM-C interacted with the Golgi reassembly stacking protein of 55 kDa (GRASP55, encoded by Gorasp2) in developing germ cells. Generation and study of Gorasp2-/- mice revealed that knock-out mice suffered from spermatogenesis defects. Acrosome formation and polarized localization of JAM-C in spermatids were altered in Gorasp2-/- mice. In addition, Golgi morphology of spermatocytes was disturbed in Gorasp2-/- mice. Crystal structures of GRASP55 in complex with JAM-C or JAM-B revealed that GRASP55 interacted via PDZ-mediated interactions with JAMs and induced a conformational change in GRASP55 with respect of its free conformation. An in silico pharmacophore approach identified a chemical compound called Graspin that inhibited PDZ-mediated interactions of GRASP55 with JAMs. Treatment of mice with Graspin hampered the polarized localization of JAM-C in spermatids, induced the premature release of spermatids and affected the Golgi morphology of meiotic spermatocytes.

Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis.,Cartier-Michaud A, Bailly AL, Betzi S, Shi X, Lissitzky JC, Zarubica A, Serge A, Roche P, Lugari A, Hamon V, Bardin F, Derviaux C, Lembo F, Audebert S, Marchetto S, Durand B, Borg JP, Shi N, Morelli X, Aurrand-Lions M PLoS Genet. 2017 Jun 15;13(6):e1006803. doi: 10.1371/journal.pgen.1006803., eCollection 2017 Jun. PMID:28617811^[2]

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

References

↑ Shorter J, Watson R, Giannakou ME, Clarke M, Warren G, Barr FA. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J. 1999 Sep 15;18(18):4949-60. PMID:10487747 doi:http://dx.doi.org/10.1093/emboj/18.18.4949
↑ Cartier-Michaud A, Bailly AL, Betzi S, Shi X, Lissitzky JC, Zarubica A, Serge A, Roche P, Lugari A, Hamon V, Bardin F, Derviaux C, Lembo F, Audebert S, Marchetto S, Durand B, Borg JP, Shi N, Morelli X, Aurrand-Lions M. Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis. PLoS Genet. 2017 Jun 15;13(6):e1006803. doi: 10.1371/journal.pgen.1006803., eCollection 2017 Jun. PMID:28617811 doi:http://dx.doi.org/10.1371/journal.pgen.1006803

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5gmj"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of GRASP55 GRASP domain in complex with JAM-B C-terminus==
-<StructureSection load='5gmj' size='340' side='right' caption='[[5gmj]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
+<StructureSection load='5gmj' size='340' side='right'caption='[[5gmj]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5gmj]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GMJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5gmj]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GMJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GMJ FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gmi|5gmi]], [[5gml|5gml]]</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=5gmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gmj OCA], [http://pdbe.org/5gmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gmj RCSB], [http://www.ebi.ac.uk/pdbsum/5gmj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gmj ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gmj OCA], [http://pdbe.org/5gmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gmj RCSB], [http://www.ebi.ac.uk/pdbsum/5gmj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gmj ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Betzi, S]]
 [[Category: Huang, X]]

5gmj

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Revision as of 06:46, 13 May 2020

Crystal Structure of GRASP55 GRASP domain in complex with JAM-B C-terminus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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