|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Rlip76 (gap-gbd)== | | ==Rlip76 (gap-gbd)== |
| - | <StructureSection load='2mbg' size='340' side='right'caption='[[2mbg]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''> | + | <StructureSection load='2mbg' size='340' side='right'caption='[[2mbg]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mbg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MBG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mbg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MBG FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RALBP1, RLIP1, RLIP76 ([https://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=2mbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbg OCA], [https://pdbe.org/2mbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mbg RCSB], [https://www.ebi.ac.uk/pdbsum/2mbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbg ProSAT]</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=2mbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbg OCA], [https://pdbe.org/2mbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mbg RCSB], [https://www.ebi.ac.uk/pdbsum/2mbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RBP1_HUMAN RBP1_HUMAN]] Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin.<ref>PMID:7673236</ref> <ref>PMID:12775724</ref> <ref>PMID:11437348</ref>
| + | [https://www.uniprot.org/uniprot/RBP1_HUMAN RBP1_HUMAN] Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin.<ref>PMID:7673236</ref> <ref>PMID:12775724</ref> <ref>PMID:11437348</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Campbell, L J]] | + | [[Category: Campbell LJ]] |
| - | [[Category: Mott, H R]] | + | [[Category: Mott HR]] |
| - | [[Category: Nietlispach, D]] | + | [[Category: Nietlispach D]] |
| - | [[Category: Owen, D]] | + | [[Category: Owen D]] |
| - | [[Category: Rajasekar, K V]] | + | [[Category: Rajasekar KV]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Ralbp1]]
| + | |
| - | [[Category: Rhogap]]
| + | |
| Structural highlights
Function
RBP1_HUMAN Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin.[1] [2] [3]
Publication Abstract from PubMed
RLIP76 is an effector for Ral small GTPases, which in turn lie downstream of the master regulator Ras. Evidence is growing that Ral and RLIP76 play a role in tumorigenesis, invasion, and metastasis. RLIP76 contains both a RhoGAP domain and a Ral binding domain (GBD) and is, therefore, a node between Ras and Rho family signaling. The structure of the RhoGAP-GBD dyad reveals that the RLIP76 RhoGAP domain adopts a canonical RhoGAP domain structure and that the linker between the two RLIP76 domains is structured, fixing the orientation of the two domains and allowing RLIP76 to interact with Rho-family GTPases and Ral simultaneously. However, the juxtaposed domains do not influence each other functionally, suggesting that the RLIP76-Ral interaction controls cellular localization and that the fixed orientation of the two domains orientates the RhoGAP domain with respect to the membrane, allowing it to be perfectly poised to engage its target G proteins.
The Structure of the RLIP76 RhoGAP-Ral Binding Domain Dyad: Fixed Position of the Domains Leads to Dual Engagement of Small G Proteins at the Membrane.,Rajasekar KV, Campbell LJ, Nietlispach D, Owen D, Mott HR Structure. 2013 Oct 22. pii: S0969-2126(13)00357-2. doi:, 10.1016/j.str.2013.09.007. PMID:24207123[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH. Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J Biol Chem. 1995 Sep 22;270(38):22473-7. PMID:7673236
- ↑ Rosse C, L'Hoste S, Offner N, Picard A, Camonis J. RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis. J Biol Chem. 2003 Aug 15;278(33):30597-604. Epub 2003 May 29. PMID:12775724 doi:http://dx.doi.org/10.1074/jbc.M302191200
- ↑ Sharma R, Singhal SS, Cheng J, Yang Y, Sharma A, Zimniak P, Awasthi S, Awasthi YC. RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes. Arch Biochem Biophys. 2001 Jul 15;391(2):171-9. PMID:11437348 doi:http://dx.doi.org/10.1006/abbi.2001.2395
- ↑ Rajasekar KV, Campbell LJ, Nietlispach D, Owen D, Mott HR. The Structure of the RLIP76 RhoGAP-Ral Binding Domain Dyad: Fixed Position of the Domains Leads to Dual Engagement of Small G Proteins at the Membrane. Structure. 2013 Oct 22. pii: S0969-2126(13)00357-2. doi:, 10.1016/j.str.2013.09.007. PMID:24207123 doi:http://dx.doi.org/10.1016/j.str.2013.09.007
|
