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| | <StructureSection load='6rir' size='340' side='right'caption='[[6rir]], [[Resolution|resolution]] 1.77Å' scene=''> | | <StructureSection load='6rir' size='340' side='right'caption='[[6rir]], [[Resolution|resolution]] 1.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rir]] is a 4 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=6RIR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RIR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rir]] 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=6RIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RIR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 1.767Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAB8A, MEL, RAB8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RILPL2, RLP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6rir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rir OCA], [https://pdbe.org/6rir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rir RCSB], [https://www.ebi.ac.uk/pdbsum/6rir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rir 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=6rir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rir OCA], [http://pdbe.org/6rir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rir RCSB], [http://www.ebi.ac.uk/pdbsum/6rir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rir ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RAB8A_HUMAN RAB8A_HUMAN]] May be involved in vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization.<ref>PMID:20890297</ref> <ref>PMID:21282656</ref> [[http://www.uniprot.org/uniprot/RIPL2_HUMAN RIPL2_HUMAN]] Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). May function via activation of RAC1 and PAK1 (By similarity).[UniProtKB:Q6AYA0][UniProtKB:Q99LE1] | + | [https://www.uniprot.org/uniprot/RIPL2_HUMAN RIPL2_HUMAN] Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). May function via activation of RAC1 and PAK1 (By similarity).[UniProtKB:Q6AYA0][UniProtKB:Q99LE1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6rir" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6rir" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alessi, D R]] | + | [[Category: Alessi DR]] |
| - | [[Category: Khan, A R]] | + | [[Category: Khan AR]] |
| - | [[Category: Purlyte, E]] | + | [[Category: Purlyte E]] |
| - | [[Category: Waschbusch, D]] | + | [[Category: Waschbusch D]] |
| - | [[Category: Effector]]
| + | |
| - | [[Category: Membrane trafficking]]
| + | |
| - | [[Category: Rab gtpase]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
RIPL2_HUMAN Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). May function via activation of RAC1 and PAK1 (By similarity).[UniProtKB:Q6AYA0][UniProtKB:Q99LE1]
Publication Abstract from PubMed
Rab8a is associated with the dynamic regulation of membrane protrusions in polarized cells. Rab8a is one of several Rab GTPases that are substrates of leucine-rich repeat kinase 2 (LRRK2), a serine/threonine kinase that is linked to Parkinson's disease. Rab8a is phosphorylated at T72 (pT72) in its switch 2 helix and recruits the phospho-specific effector RILPL2, which subsequently regulates ciliogenesis. Here, we report the crystal structure of phospho-Rab8a (pRab8a) in complex with the RH2 (RILP homology) domain of RILPL2. The complex is a heterotetramer with RILPL2 forming a central alpha-helical dimer that bridges two pRab8a molecules. The N termini of the alpha helices cross over, forming an X-shaped cap (X-cap) that orients Arg residues from RILPL2 toward pT72. X-cap residues critical for pRab8a binding are conserved in JIP3 and JIP4, which also interact with LRRK2-phosphorylated Rab10. We propose a general mode of recognition for phosphorylated Rab GTPases by this family of phospho-specific effectors.
Structural Basis for Rab8a Recruitment of RILPL2 via LRRK2 Phosphorylation of Switch 2.,Waschbusch D, Purlyte E, Pal P, McGrath E, Alessi DR, Khan AR Structure. 2020 Feb 1. pii: S0969-2126(20)30005-8. doi:, 10.1016/j.str.2020.01.005. PMID:32017888[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Waschbusch D, Purlyte E, Pal P, McGrath E, Alessi DR, Khan AR. Structural Basis for Rab8a Recruitment of RILPL2 via LRRK2 Phosphorylation of Switch 2. Structure. 2020 Feb 1. pii: S0969-2126(20)30005-8. doi:, 10.1016/j.str.2020.01.005. PMID:32017888 doi:http://dx.doi.org/10.1016/j.str.2020.01.005
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