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2xze

From Proteopedia

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Structural basis for AMSH-ESCRT-III CHMP3 interaction

Structural highlights

2xze is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.75Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

STABP_HUMAN Microcephaly-capillary malformation syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

STABP_HUMAN Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Endosomal sorting complexes required for transport (ESCRT) recognize ubiquitinated cargo and catalyze diverse budding processes including multivesicular body biogenesis, enveloped virus egress, and cytokinesis. We present the crystal structure of an N-terminal fragment of the deubiquitinating enzyme AMSH (AMSHDeltaC) in complex with the C-terminal region of ESCRT-III CHMP3 (CHMP3DeltaN). AMSHDeltaC folds into an elongated 90 A long helical assembly that includes an unusual MIT domain. CHMP3DeltaN is unstructured in solution and helical in complex with AMSHDeltaC, revealing a novel MIT domain interacting motif (MIM) that does not overlap with the CHMP1-AMSH binding site. ITC and SPR measurements demonstrate an unusual high-affinity MIM-MIT interaction. Structural analysis suggests a regulatory role for the N-terminal helical segment of AMSHDeltaC and its destabilization leads to a loss of function during HIV-1 budding. Our results indicate a tight coupling of ESCRT-III CHMP3 and AMSH functions and provide insight into the regulation of ESCRT-III.

Structural Basis for ESCRT-III CHMP3 Recruitment of AMSH.,Solomons J, Sabin C, Poudevigne E, Usami Y, Hulsik DL, Macheboeuf P, Hartlieb B, Gottlinger H, Weissenhorn W Structure. 2011 Aug 10;19(8):1149-59. PMID:21827950^[6]

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

References

↑ Tanaka N, Kaneko K, Asao H, Kasai H, Endo Y, Fujita T, Takeshita T, Sugamura K. Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines. J Biol Chem. 1999 Jul 2;274(27):19129-35. PMID:10383417
↑ Itoh F, Asao H, Sugamura K, Heldin CH, ten Dijke P, Itoh S. Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads. EMBO J. 2001 Aug 1;20(15):4132-42. PMID:11483516 doi:http://dx.doi.org/10.1093/emboj/20.15.4132
↑ McCullough J, Clague MJ, Urbe S. AMSH is an endosome-associated ubiquitin isopeptidase. J Cell Biol. 2004 Aug 16;166(4):487-92. PMID:15314065 doi:http://dx.doi.org/10.1083/jcb.200401141
↑ Ma YM, Boucrot E, Villen J, Affar el B, Gygi SP, Gottlinger HG, Kirchhausen T. Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation. J Biol Chem. 2007 Mar 30;282(13):9805-12. Epub 2007 Jan 29. PMID:17261583 doi:http://dx.doi.org/10.1074/jbc.M611635200
↑ McDonell LM, Mirzaa GM, Alcantara D, Schwartzentruber J, Carter MT, Lee LJ, Clericuzio CL, Graham JM Jr, Morris-Rosendahl DJ, Polster T, Acsadi G, Townshend S, Williams S, Halbert A, Isidor B, David A, Smyser CD, Paciorkowski AR, Willing M, Woulfe J, Das S, Beaulieu CL, Marcadier J, Geraghty MT, Frey BJ, Majewski J, Bulman DE, Dobyns WB, O'Driscoll M, Boycott KM. Mutations in STAMBP, encoding a deubiquitinating enzyme, cause microcephaly-capillary malformation syndrome. Nat Genet. 2013 May;45(5):556-62. doi: 10.1038/ng.2602. Epub 2013 Mar 31. PMID:23542699 doi:http://dx.doi.org/10.1038/ng.2602
↑ Solomons J, Sabin C, Poudevigne E, Usami Y, Hulsik DL, Macheboeuf P, Hartlieb B, Gottlinger H, Weissenhorn W. Structural Basis for ESCRT-III CHMP3 Recruitment of AMSH. Structure. 2011 Aug 10;19(8):1149-59. PMID:21827950 doi:10.1016/j.str.2011.05.011

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xze"

Categories: Homo sapiens | Large Structures | Sabin C | Solomons J | Weissenhorn W

@@ Line 1: / Line 1: @@
-==STRUCTURAL BASIS FOR AMSH-ESCRT-III CHMP3 INTERACTION==
-<StructureSection load='2xze' size='340' side='right' caption='[[2xze]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+==Structural basis for AMSH-ESCRT-III CHMP3 interaction==
+<StructureSection load='2xze' size='340' side='right'caption='[[2xze]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xze]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XZE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xze]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XZE FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gd5|2gd5]]</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]] 1.75&#8491;</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=2xze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xze RCSB], [http://www.ebi.ac.uk/pdbsum/2xze PDBsum]</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=2xze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xze OCA], [https://pdbe.org/2xze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xze RCSB], [https://www.ebi.ac.uk/pdbsum/2xze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xze ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/STABP_HUMAN STABP_HUMAN] Microcephaly-capillary malformation syndrome. The disease is caused by mutations affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/STABP_HUMAN STABP_HUMAN] Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.<ref>PMID:10383417</ref> <ref>PMID:11483516</ref> <ref>PMID:15314065</ref> <ref>PMID:17261583</ref> <ref>PMID:23542699</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2xze" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[ATPase|ATPase]]
+*[[ATPase 3D structures|ATPase 3D structures]]
+*[[Charged multivesicular body protein 3D structures|Charged multivesicular body protein 3D structures]]
 == References ==
 <references/>
@@ Line 22: / Line 29: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Sabin, C.]]
+[[Category: Large Structures]]
-[[Category: Solomons, J.]]
+[[Category: Sabin C]]
-[[Category: Weissenhorn, W.]]
+[[Category: Solomons J]]
-[[Category: Hydrolase-protein transport complex]]
+[[Category: Weissenhorn W]]

2xze

From Proteopedia

Current revision

Structural basis for AMSH-ESCRT-III CHMP3 interaction

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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