4xc2 | pdb_00004xc2

Crystal structure of GABARAP in complex with KBTBD6 LIR peptide

spinqualitylabelsall models 4xc2, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Method: X-ray diffraction, Resolution 1.9Å 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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also GABA receptor-associated protein 3D structures GABA(A) receptor-associated protein

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