Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome

References

• Attree O, Olivos IM, Okabe I, Bailey LC, Nelson DL, Lewis RA, et al. The Lowe’s oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature 1992; 358:239 - 42; http://dx.doi.org/10.1038/358239a0; PMID: 1321346
   PubMed Web of Science ®Google Scholar
• Schurman SJ, Scheinman SJ. Inherited cerebrorenal syndromes. Nat Rev Nephrol 2009; 5:529 - 38; http://dx.doi.org/10.1038/nrneph.2009.124; PMID: 19701229
   PubMed Web of Science ®Google Scholar
• Choudhury R, Diao A, Zhang F, Eisenberg E, Saint-Pol A, Williams C, et al. Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network. Mol Biol Cell 2005; 16:3467 - 79; http://dx.doi.org/10.1091/mbc.E05-02-0120; PMID: 15917292
   PubMed Web of Science ®Google Scholar
• Coon BG, Mukherjee D, Hanna CB, Riese DJ 2nd, Lowe M, Aguilar RC. Lowe syndrome patient fibroblasts display Ocrl1-specific cell migration defects that cannot be rescued by the homologous Inpp5b phosphatase. Hum Mol Genet 2009; 18:4478 - 91; http://dx.doi.org/10.1093/hmg/ddp407; PMID: 19700499
   PubMed Web of Science ®Google Scholar
• Noakes CJ, Lee G, Lowe M. The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway. Mol Biol Cell 2011; 22:606 - 23; http://dx.doi.org/10.1091/mbc.E10-08-0730; PMID: 21233288
   PubMed Web of Science ®Google Scholar
• Vicinanza M, Di Campli A, Polishchuk E, Santoro M, Di Tullio G, Godi A, et al. OCRL controls trafficking through early endosomes via PtdIns4,5P₂-dependent regulation of endosomal actin. EMBO J 2011; 30:4970 - 85; http://dx.doi.org/10.1038/emboj.2011.354; PMID: 21971085
   PubMed Web of Science ®Google Scholar
• Erdmann KS, Mao Y, McCrea HJ, Zoncu R, Lee S, Paradise S, et al. A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway. Dev Cell 2007; 13:377 - 90; http://dx.doi.org/10.1016/j.devcel.2007.08.004; PMID: 17765681
   PubMed Web of Science ®Google Scholar
• Mao Y, Balkin DM, Zoncu R, Erdmann KS, Tomasini L, Hu F, et al. A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism. EMBO J 2009; 28:1831 - 42; http://dx.doi.org/10.1038/emboj.2009.155; PMID: 19536138
   PubMed Web of Science ®Google Scholar
• Choudhury R, Noakes CJ, McKenzie E, Kox C, Lowe M. Differential clathrin binding and subcellular localization of OCRL1 splice isoforms. J Biol Chem 2009; 284:9965 - 73; http://dx.doi.org/10.1074/jbc.M807442200; PMID: 19211563
   PubMed Web of Science ®Google Scholar
• Ungewickell A, Ward ME, Ungewickell E, Majerus PW. The inositol polyphosphate 5-phosphatase Ocrl associates with endosomes that are partially coated with clathrin. Proc Natl Acad Sci U S A 2004; 101:13501 - 6; http://dx.doi.org/10.1073/pnas.0405664101; PMID: 15353600
   PubMed Web of Science ®Google Scholar
• Swan LE, Tomasini L, Pirruccello M, Lunardi J, De Camilli P. Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1. Proc Natl Acad Sci U S A 2010; 107:3511 - 6; http://dx.doi.org/10.1073/pnas.0914658107; PMID: 20133602
   PubMed Web of Science ®Google Scholar
• Fukuda M, Kanno E, Ishibashi K, Itoh T. Large scale screening for novel rab effectors reveals unexpected broad Rab binding specificity. Mol Cell Proteomics 2008; 7:1031 - 42; http://dx.doi.org/10.1074/mcp.M700569-MCP200; PMID: 18256213
   PubMed Web of Science ®Google Scholar
• Hyvola N, Diao A, McKenzie E, Skippen A, Cockcroft S, Lowe M. Membrane targeting and activation of the Lowe syndrome protein OCRL1 by rab GTPases. EMBO J 2006; 25:3750 - 61; http://dx.doi.org/10.1038/sj.emboj.7601274; PMID: 16902405
   PubMed Web of Science ®Google Scholar
• Hou X, Hagemann N, Schoebel S, Blankenfeldt W, Goody RS, Erdmann KS, et al. Structural basis for Lowe syndrome caused by mutations in the Rab binding domain of OCRL1. EMBO J 2011; 30:1659 - 70; http://dx.doi.org/10.1002/humu.9239; PMID: 15108291
   PubMed Web of Science ®Google Scholar
• Merithew E, Hatherly S, Dumas JJ, Lawe DC, Heller-Harrison R, Lambright DG. Structural plasticity of an invariant hydrophobic triad in the switch regions of Rab GTPases is a determinant of effector recognition. J Biol Chem 2001; 276:13982 - 8; PMID: 11278565
   PubMed Web of Science ®Google Scholar
• Pirruccello M, Swan LE, Folta-Stogniew E, De Camilli P. Recognition of the F&H motif by the Lowe syndrome protein OCRL. Nat Struct Mol Biol 2011; 18:789 - 95; http://dx.doi.org/10.1038/nsmb.2071; PMID: 21666675
   PubMed Web of Science ®Google Scholar
• Peränen J. Rab8 GTPase as a regulator of cell shape. Cytoskeleton (Hoboken) 2011; 68:527 - 39; http://dx.doi.org/10.1002/cm.20529; PMID: 21850707
   PubMed Web of Science ®Google Scholar
• Bockenhauer D, Bokenkamp A, van’t Hoff W, Levtchenko E, Kist-van Holthe JE, Tasic V, et al. Renal phenotype in Lowe Syndrome: a selective proximal tubular dysfunction. Clin J Am Soc Nephrol 2008; 3:1430 - 6; http://dx.doi.org/10.2215/CJN.00520108; PMID: 18480301
   PubMed Web of Science ®Google Scholar
• Norden AG, Lapsley M, Igarashi T, Kelleher CL, Lee PJ, Matsuyama T, et al. Urinary megalin deficiency implicates abnormal tubular endocytic function in Fanconi syndrome. J Am Soc Nephrol 2002; 13:125 - 33; PMID: 11752029
   PubMed Web of Science ®Google Scholar
• Sato T, Mushiake S, Kato Y, Sato K, Sato M, Takeda N, et al. The Rab8 GTPase regulates apical protein localization in intestinal cells. Nature 2007; 448:366 - 9; http://dx.doi.org/10.1038/nature05929; PMID: 17597763
   PubMed Web of Science ®Google Scholar
• Ang AL, Fölsch H, Koivisto UM, Pypaert M, Mellman I. The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells. J Cell Biol 2003; 163:339 - 50; http://dx.doi.org/10.1083/jcb.200307046; PMID: 14581456
   PubMed Web of Science ®Google Scholar
• Huber LA, Pimplikar S, Parton RG, Virta H, Zerial M, Simons K. Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J Cell Biol 1993; 123:35 - 45; http://dx.doi.org/10.1083/jcb.123.1.35; PMID: 8408203
   PubMed Web of Science ®Google Scholar
• Henry L, Sheff DR. Rab8 regulates basolateral secretory, but not recycling, traffic at the recycling endosome. Mol Biol Cell 2008; 19:2059 - 68; http://dx.doi.org/10.1091/mbc.E07-09-0902; PMID: 18287531
   PubMed Web of Science ®Google Scholar
• Hattula K, Furuhjelm J, Tikkanen J, Tanhuanpää K, Laakkonen P, Peränen J. Characterization of the Rab8-specific membrane traffic route linked to protrusion formation. J Cell Sci 2006; 119:4866 - 77; http://dx.doi.org/10.1242/jcs.03275; PMID: 17105768
   PubMed Web of Science ®Google Scholar
• Huber LA, Dupree P, Dotti CG. A deficiency of the small GTPase rab8 inhibits membrane traffic in developing neurons. Mol Cell Biol 1995; 15:918 - 24; PMID: 7823956
   PubMed Web of Science ®Google Scholar
• Gerges NZ, Backos DS, Esteban JA. Local control of AMPA receptor trafficking at the postsynaptic terminal by a small GTPase of the Rab family. J Biol Chem 2004; 279:43870 - 8; http://dx.doi.org/10.1074/jbc.M404982200; PMID: 15297461
   PubMed Web of Science ®Google Scholar
• Nachury MV, Loktev AV, Zhang Q, Westlake CJ, Peränen J, Merdes A, et al. A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis. Cell 2007; 129:1201 - 13; http://dx.doi.org/10.1016/j.cell.2007.03.053; PMID: 17574030
   PubMed Web of Science ®Google Scholar
• Ponting CP. A novel domain suggests a ciliary function for ASPM, a brain size determining gene. Bioinformatics 2006; 22:1031 - 5; http://dx.doi.org/10.1093/bioinformatics/btl022; PMID: 16443634
   PubMed Web of Science ®Google Scholar