4xc2

From Proteopedia

(Difference between revisions)

Revision as of 21:21, 12 April 2023

Crystal structure of GABARAP in complex with KBTBD6 LIR peptide

Structural highlights

4xc2 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GBRAP_HUMAN May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy (By similarity).^[1]

Publication Abstract from PubMed

The small Rho GTPase RAC1 is an essential regulator of cellular signaling that controls actin rearrangements and cell motility. Here, we identify a novel CUL3 RING ubiquitin ligase complex, containing the substrate adaptors KBTBD6 and KBTBD7, that mediates ubiquitylation and proteasomal degradation of TIAM1, a RAC1-specific GEF. Increasing the abundance of TIAM1 by depletion of KBTBD6 and/or KBTBD7 leads to elevated RAC1 activity, changes in actin morphology, loss of focal adhesions, reduced proliferation, and enhanced invasion. KBTBD6 and KBTBD7 employ ATG8 family-interacting motifs to bind preferentially to GABARAP proteins. Surprisingly, ubiquitylation and degradation of TIAM1 by CUL3KBTBD6/KBTBD7 depends on its binding to GABARAP proteins. Our study reveals that recruitment of CUL3KBTBD6/KBTBD7 to GABARAP-containing vesicles regulates the abundance of membrane-associated TIAM1 and subsequently spatially restricted RAC1 signaling. Besides their role in autophagy and trafficking, we uncovered a previously unknown function of GABARAP proteins as membrane-localized signaling scaffolds.

CUL3-KBTBD6/KBTBD7 Ubiquitin Ligase Cooperates with GABARAP Proteins to Spatially Restrict TIAM1-RAC1 Signaling.,Genau HM, Huber J, Baschieri F, Akutsu M, Dotsch V, Farhan H, Rogov V, Behrends C Mol Cell. 2015 Feb 11. pii: S1097-2765(14)01018-1. doi:, 10.1016/j.molcel.2014.12.040. PMID:25684205^[2]

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

References

↑ Lee JH, Rho SB, Chun T. GABAA receptor-associated protein (GABARAP) induces apoptosis by interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47). Biotechnol Lett. 2005 May;27(9):623-8. PMID:15977068 doi:http://dx.doi.org/10.1007/s10529-005-3628-2
↑ Genau HM, Huber J, Baschieri F, Akutsu M, Dotsch V, Farhan H, Rogov V, Behrends C. CUL3-KBTBD6/KBTBD7 Ubiquitin Ligase Cooperates with GABARAP Proteins to Spatially Restrict TIAM1-RAC1 Signaling. Mol Cell. 2015 Feb 11. pii: S1097-2765(14)01018-1. doi:, 10.1016/j.molcel.2014.12.040. PMID:25684205 doi:http://dx.doi.org/10.1016/j.molcel.2014.12.040

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xc2"

@@ Line 3: / Line 3: @@
 <StructureSection load='4xc2' size='340' side='right'caption='[[4xc2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4xc2]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XC2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4xc2]] is a 8 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=4XC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XC2 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GABARAP, hCG_1987397 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=4xc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xc2 OCA], [https://pdbe.org/4xc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xc2 RCSB], [https://www.ebi.ac.uk/pdbsum/4xc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xc2 ProSAT]</span></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=4xc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xc2 OCA], [http://pdbe.org/4xc2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4xc2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xc2 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GBRAP_HUMAN GBRAP_HUMAN] May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy (By similarity).<ref>PMID:15977068</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 ==See Also==
+*[[GABA receptor-associated protein 3D structures|GABA receptor-associated protein 3D structures]]
 *[[GABA(A) receptor-associated protein|GABA(A) receptor-associated protein]]
 == References ==
@@ Line 23: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Akutsu, M]]
+[[Category: Akutsu M]]
-[[Category: Baschieri, F]]
+[[Category: Baschieri F]]
-[[Category: Behrends, C]]
+[[Category: Behrends C]]
-[[Category: Doetsch, V]]
+[[Category: Doetsch V]]
-[[Category: Farhan, H]]
+[[Category: Farhan H]]
-[[Category: Genau, H M]]
+[[Category: Genau HM]]
-[[Category: Huber, J]]
+[[Category: Huber J]]
-[[Category: Rogov, V V]]
+[[Category: Rogov VV]]
-[[Category: Autophagy]]
-[[Category: Complex]]
-[[Category: Immune system]]

4xc2

From Proteopedia

Revision as of 21:21, 12 April 2023

Crystal structure of GABARAP in complex with KBTBD6 LIR peptide

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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