Septin 7 forms a complex with CD2AP and nephrin and regulates glucose transporter trafficking

Molecular Biology of the Cell

Volumn 23, Issue 17, 2012, Pages 3370-3379

  Wasik, Anita A ^a   Polianskyte Prause, Zydrune ^a   Dong, Meng Qiu ^b   Shaw, Andrey S ^c   Yates III, John R ^b   Farquhar, Marilyn G ^d   Lehtonen, Sanna ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CARBANILAMIDE DERIVATIVE; CD2 ASSOCIATED PROTEIN; DEOXYGLUCOSE; FORCHLORFENURON; GLUCOSE TRANSPORTER; GLUCOSE TRANSPORTER 4; NEPHRIN; PHOSPHATIDYLINOSITOL 3 KINASE; SEPTIN; SEPTIN 11; SEPTIN 7; SEPTIN 9; SMALL INTERFERING RNA; SYNAPTOBREVIN 2; SYNTAXIN 4; UNCLASSIFIED DRUG;

ACTIN FILAMENT; ANIMAL CELL; ARTICLE; CELL FRACTIONATION; CELL MEMBRANE; CELL VACUOLE; COMPLEX FORMATION; CONTROLLED STUDY; CYTOPLASM; ENZYME ACTIVITY; GENE SILENCING; GLOMERULUS FILTRATION; GLUCOSE TRANSPORT; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE MICROSCOPY; IMMUNOPRECIPITATION; MALE; MOUSE; NONHUMAN; PODOCYTE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEPLETION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; ULTRAFILTRATION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; CELL MEMBRANE; CELLS, CULTURED; CYTOSKELETAL PROTEINS; GLUCOSE TRANSPORTER TYPE 4; HUMANS; INSULIN; MEMBRANE PROTEINS; MICE; PHENYLUREA COMPOUNDS; PODOCYTES; PROTEIN TRANSPORT; PYRIDINES; QA-SNARE PROTEINS; RATS; RATS, SPRAGUE-DAWLEY; RNA INTERFERENCE; RNA, SMALL INTERFERING; SEPTINS; VESICLE-ASSOCIATED MEMBRANE PROTEIN 2;

EID: 84865765262     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E11-12-1010     Document Type: Article

References (48)

1. Ahola H, Heikkila E, Astrom E, Inagaki M, Izawa I, Pavenstadt H, Kerjaschki D, Holthofer H (2003). A novel protein, densin, expressed by glomerular podocytes. J Am Soc Nephrol 14, 1731-1737.
2. Beites CL, Campbell KA, Trimble WS (2005). The septin Sept5/CDCrel-1 competes with α-SNAP for binding to the SNARE complex. Biochem J 385, 347-353.
3. Beites CL, Xie H, Bowser R, Trimble WS (1999). The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat Neurosci 2, 434-439.
4. Cormont M, Meton I, Mari M, Monzo P, Keslair F, Gaskin C, McGraw TE, Le Marchand-Brustel Y (2003). CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl. Traffic 4, 97-112.
5. Coward RJ, Welsh GI, Koziell A, Hussain S, Lennon R, Ni L, Tavare JM, Mathieson PW, Saleem MA (2007). Nephrin is critical for the action of insulin on human glomerular podocytes. Diabetes 56, 1127-1135.
6. Coward RJ et al. (2005). The human glomerular podocyte is a novel target for insulin action. Diabetes 54, 3095-3102.
7. Dustin ML et al. (1998). A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts. Cell 94, 667-677.
8. Eng JK, McCormack AL, Yates JR, III (1994). An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5, 976-89.
9. Haarer BK, Pringle JR (1987). Immunofluorescence localization of the Saccharomyces cerevisiae CDC12 gene product to the vicinity of the 10-nm filaments in the mother-bud neck. Mol Cell Biol 7, 3678-3687.
10. Hall PA, Jung K, Hillan KJ, Russell SE (2005). Expression profiling the human septin gene family. J Pathol 206, 269-278.
11. Hall PA, Russell SE (2004). The pathobiology of the septin gene family. J Pathol 204, 489-505.
12. Hartwell LH (1971). Genetic control of the cell division cycle in yeast. IV: Genes controlling bud emergence and cytokinesis. Exp Cell Res 69, 265-276.
13. Hsu SC, Hazuka CD, Roth R, Foletti DL, Heuser J, Scheller RH (1998). Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron 20, 1111-1122.
14. Hu Q, Nelson WJ, Spiliotis ET (2008). Forchlorfenuron alters mammalian septin assembly, organization, and dynamics. J Biol Chem 283, 29563-29571.
15. Iwase M, Okada S, Oguchi T, Toh-e A (2004). Forchlorfenuron, a phenylurea cytokine, disturbs septin organization in Saccharomyces cerevisiae. Genes Genet Syst 79, 199-206.
16. Joberty G, Perlungher RR, Sheffield PJ, Kinoshita M, Noda M, Haystead T, Macara IG (2001). Borg proteins control septin organization and are negatively regulated by Cdc42. Nat Cell Biol 3, 861-866.
17. Kestila M et al. (1998). Positionally cloned gene for a novel glomerular protein-nephrin-is mutated in congenital nephrotic syndrome. Mol Cell 1, 575-582.
18. Kim HB, Haarer BK, Pringle JR (1991). Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC3 gene product and the timing of events at the budding site. J Cell Biol 112, 535-544.
19. Kinoshita M (2003). The septins. Genome Biol 4, 236.
20. Kinoshita M, Field CM, Coughlin ML, Straight AF, Mitchison TJ (2002). Self- and actin-templated assembly of mammalian septins. Dev Cell 3, 791-802.
21. Kinoshita M, Kumar S, Mizoguchi A, Ide C, Kinoshita A, Haraguchi T, Hiraoka Y, Noda M (1997). Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures. Genes Dev 11, 1535-1547.
22. Kirsch KH, Georgescu MM, Shishido T, Langdon WY, Birge RB, Hanafusa H (2001). The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction. J Biol Chem 276, 4957-4963.
23. Kremer BE, Adang LA, Macara IG (2007). Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7. Cell 130, 837-850.
24. Lehtonen S, Lehtonen E, Kudlicka K, Holthofer H, Farquhar MG (2004). Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin. Am J Pathol 165, 923-936.
25. Lehtonen S, Ora A, Olkkonen VM, Geng L, Zerial M, Somlo S, Lehtonen E (2000). In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2. J Biol Chem 275, 32888-32893.
26. Lehtonen S, Shah M, Nielsen R, Iino N, Ryan JJ, Zhou H, Farquhar MG (2008a). The endocytic adaptor protein ARH associates with motor and centrosomal proteins and is involved in centrosome assembly and cytokinesis. Mol Biol Cell 19, 2949-2961.
27. Lehtonen S, Tienari J, Londesborough A, Pirvola U, Ora A, Reima I, Lehtonen E (2008b). CD2-associated protein is widely expressed and differentially regulated during embryonic development. Differentiation 76, 506-517.
28. Lehtonen S, Zhao F, Lehtonen E (2002). CD2-associated protein directly interacts with the actin cytoskeleton. Am J Physiol Renal Physiol 283, F734-F43.
29. Monzo P, Gauthier NC, Keslair F, Loubat A, Field CM, Le Marchand-Brustel Y, Cormont M (2005). Clues to CD2-associated protein involvement in cytokinesis. Mol Biol Cell 16, 2891-2902.
30. Nagata K, Asano T, Nozawa Y, Inagaki M (2004). Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11. J Biol Chem 279, 55895-55904.
31. Oegema K, Savoian MS, Mitchison TJ, Field CM (2000). Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis. J Cell Biol 150, 539-552.
32. Orlando RA, Takeda T, Zak B, Schmieder S, Benoit VM, McQuistan T, Furthmayr H, Farquhar MG (2001). The glomerular epithelial cell anti-adhesin podocalyxin associates with the actin cytoskeleton through interactions with ezrin. J Am Soc Nephrol 12, 1589-1598.
33. Palmen T, Lehtonen S, Ora A, Kerjaschki D, Antignac C, Lehtonen E, Holthofer H (2002). Interaction of endogenous nephrin and CD2-associated protein in mouse epithelial M-1 cell line. J Am Soc Nephrol 13, 1766-1772.
34. Rothman JE (1994). Intracellular membrane fusion. Adv Second Messenger Phosphoprotein Res 29, 81-96.
35. Saleem MA, O'Hare MJ, Reiser J, Coward RJ, Inward CD, Farren T, Xing CY, Ni L, Mathieson PW, Mundel P (2002). A conditionally immortalized human podocyte cell line demonstrating nephrin and podocin expression. J Am Soc Nephrol 13, 630-638.
36. Schiffer M, Mundel P, Shaw AS, Bottinger EP (2004). A novel role for the adaptor molecule CD2-associated protein in transforming growth factor-β-induced apoptosis. J Biol Chem 279, 37004-37012.
37. Schmidt K, Nichols BJ (2004). Functional interdependence between septin and actin cytoskeleton. BMC Cell Biol 5, 43.
38. Shankland SJ (2006). The podocyte's response to injury: role in proteinuria and glomerulosclerosis. Kidney Int 69, 2131-2147.
39. Shih NY, Li J, Cotran R, Mundel P, Miner JH, Shaw AS (2001). CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain. Am J Pathol 159, 2303-2308.
40. Shih NY, Li J, Karpitskii V, Nguyen A, Dustin ML, Kanagawa O, Miner JH, Shaw AS (1999). Congenital nephrotic syndrome in mice lacking CD2-associated protein. Science 286, 312-315.
41. Söllner T, Whiteheart SW, Brunner M, Erdjument-Bromage H, Geromanos S, Tempst P, Rothman JE (1993). SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324.
42. Tabb DL, McDonald WH, Yates JR, III (2002). DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1, 21-26.
43. Tejada T, Catanuto P, Ijaz A, Santos JV, Xia X, Sanchez P, Sanabria N, Lenz O, Elliot SJ, Fornoni A (2008). Failure to phosphorylate AKT in podocytes from mice with early diabetic nephropathy promotes cell death. Kidney Int 73, 1385-1393.
44. Vega IE, Hsu SC (2003). The septin protein Nedd5 associates with both the exocyst complex and microtubules and disruption of its GTPase activity promotes aberrant neurite sprouting in PC12 cells. Neuroreport 14, 31-37.
45. Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Sollner TH, Rothman JE (1998). SNAREpins: minimal machinery for membrane fusion. Cell 92, 759-772.
46. Welsch T, Endlich N, Kriz W, Endlich K (2001). CD2AP and p130Cas localize to different F-actin structures in podocytes. Am J Physiol Renal Physiol 281, F769-F77.
47. Welsh GI et al. (2010). Insulin signaling to the glomerular podocyte is critical for normal kidney function. Cell Metab 12, 329-340.
48. Yaddanapudi S et al. (2011). CD2AP in mouse and human podocytes controls a proteolytic program that regulates cytoskeletal structure and cellular survival. J Clin Invest. 121, 3965-3980.