Nedd4, a human ubiquitin ligase, affects actin cytoskeleton in yeast cells

Experimental Cell Research

Volumn 314, Issue 18, 2008, Pages 3318-3325

  Stawiecka Mirota, Marta ^a,b   Kamińska, Joanna ^a   Urban Grimal, Daniele ^b   Haines, Dale S ^c   Zoładek, Teresa ^a  

^a INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^b INSTITUT JACQUES MONOD   (France)

^c TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Actin cytoskeleton organization; Latrunculin A; Ubiquitin ligase; Yeast

Indexed keywords

ACTIN; LATRUNCULIN A; UBIQUITIN PROTEIN LIGASE NEDD4;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CYTOSKELETON; GENE EXPRESSION; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION; YEAST CELL;

EID: 54349108063     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.08.017     Document Type: Article

References (49)

1. Fang S., and Weissman A.M. A field guide to ubiquitylation. Cell. Mol. Life Sci. 61 (2004) 1546-1561
2. Ingham R.J., Gish G., and Pawson T. The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture. Oncogene 23 (2004) 1972-1984
3. Kumar S., Tomooka Y., and Noda M. Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem. Biophys. Res. Com. 185 (1992) 1155-1161
4. Shearwin-Whyatt L., Dalton H.E., Foot N., and Kumar S. Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins. BioEssays 28 (2006) 617-628
5. Wang X., Trotman L.C., Koppie T., Alimonti A., Chen Z., Gao Z., Wang J., Erdjument-Bromage H., Tempst P., Cordon-Cardo C., Pandolfi P.P., and Jiang X. NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell 128 (2007) 129-139
6. Hamilton K.L., and Butt A.G. The molecular basis of renal tubular transport disorders. Comp. Biochem. Physiol. 126 (2000) 305-321
7. Rotin D., Staub O., and Haguenauer-Tsapis R. Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J. Membr. Biol. 176 (2000) 1-17
8. Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., and Basyuk E. Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding. J. Biol. Chem. 280 (2005) 27004-27012
9. Beaudenon S.L., Huacani M.R., Wang G., McDonnell D.P., and Huibregtse J.M. Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae. Mol. Cell. Biol. 19 (1999) 6972-6979
10. Neumann S., Petfalski E., Brugger B., Grosshans H., Wieland F., Tollervey D., and Hurt E. Formation and nuclear export of tRNA, rRNA and mRNA is regulated by the ubiquitin ligase Rsp5p. EMBO Rep. 4 (2003) 1156-1162
11. Rodriguez M.S., Gwizdek C., Haguenauer-Tsapis R., and Dargemont C. The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae. Traffic 4 (2003) 566-575
12. Kwapisz M., Cholbinski P., Hopper A.K., Rousset J.P., and Żoła{ogonek}dek T. Rsp5 ubiquitin ligase modulates translation accuracy in yeast Saccharomyces cerevisiae. RNA 11 (2005) 1710-1718
13. Hoppe T., Matuschewski K., Rape M., Schlenker S., Ulrich H.D., and Jentsch S. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102 (2000) 577-586
14. Shcherbik N., Kumar S., and Haines D.S. Substrate proteolysis is inhibited by dominant-negative Nedd4 and Rsp5 mutants harboring alterations in WW domain 1. J. Cell. Sci. 115 (2002) 1041-1048
15. Engqvist-Goldstein A.E., and Drubin D.G. Actin assembly and endocytosis: from yeast to mammals. Ann. Rev. Cell Dev. Biol. 19 (2003) 287-332
16. Li R. Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J. Cell Biol. 136 (1997) 649-658
17. Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C., Soulard A., Moreau V., and Winsor B. The Saccharomyces cerevisiae-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex. Mol. Biol. Cell 10 (1999) 3521-3538
18. Winter D., Lechler T., and Li R. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9 (1999) 501-504
19. Kamińska J., Gajewska B., Hopper A.K., and Żoła{ogonek}dek T. Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 22 (2002) 6946-6948
20. Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., and Gygi S.P. A proteomics approach to understanding protein ubiquitination. Nature Biotech. 21 (2003) 921-926
21. Hitchcock A.L., Auld K., Gygi S.P., and Silver P.A. A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 12735-12740
22. Gupta R., Kus B., Fladd C., Wasmuth J., Tonikian R., Sidhu S., Krogan N.J., Parkinson J., and Rotin D. Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast. Mol. Syst. Biol. 3 (2007) 116
23. Gajewska B., Shcherbik N., Oficjalska D., Haines D.S., and Żoła{ogonek}dek T. Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast. Curr. Genet. 43 (2003) 1-10
24. Moreau V., Madania A., Martin R.P., and Winson B. The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J. Cell Biol. 134 (1996) 117-132
25. Katzmann D.J., and Wendland B. Analysis of ubiquitin-dependent protein sorting within the endocytic pathway in Saccharomyces cerevisiae. Methods Enzymol. 399 (2005) 192-211
26. Ayscough K.R., Stryker J., Pokala N., Sanders M., Crews P., and Drubin D.G. High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 137 (1997) 399-416
27. Tong A.H., Drees B., Nardelli G., Bader G.D., Brannetti B., Castagnoli L., Evangelista M., Ferracuti S., Nelson B., Paoluzi S., Quondam M., Zucconi A., Hogue C.W., Fields S., Boone C., and Cesareni G. A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 295 (2002) 321-324
28. Foury F. Human genetic diseases: a cross-talk between man and yeast. Gene 195 (1997) 1-10
29. Witt S.N., and Flower T.R. alpha-Synuclein, oxidative stress and apoptosis from the perspective of a yeast model of Parkinson's disease. FEMS Yeast Res. 6 (2006) 1107-1116
30. Pruyne D., and Bretscher A. Polarization of cell growth in yeast. I. Establishment and maintenance of polarity states. J. Cell Sci. 113 (2000) 365-375
31. Pruyne D., and Bretscher A. Polarization of cell growth in yeast II. The role of the cortical actin cytoskeleton. J. Cell Sci. 113 (2000) 571-585
32. Lu J.Y., Lin Y.Y., Qian J., Tao S.C., Zhu J., Pickart C., and Zhu H. Functional dissection of a HECT ubiquitin E3 ligase. Mol. Cell. Proteomics 7 (2008) 35-45
33. Stamenova S.D., Dunn R., Adler A.S., and Hicke L. The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167. J. Biol. Chem. 279 (2004) 16017-16025
34. Haglund K., Shimokawa N., Szymkiewicz I., and Dikic I. Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 12191-12196
35. Ren G., Vajjhala P., Lee J.S., Winsor B., and Munn A.L. The BAR domain proteins: molding membranes in fission, fusion, and phagy. Micro. Mol. Biol. Rev. 70 (2006) 37-120
36. Gavin A.C., Bosche M., Krause R., Grandi P., Marzioch M., Bauer A., Schultz J., Rick J.M., Michon A.M., Cruciat C.M., Remor M., Hofert C., Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M., Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C., Heurtier M.A., Copley R.R., Edelmann A., Querfurth E., Rybin V., Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B., Neubauer G., and Superti-Furga G. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415 (2002) 141-147
37. Gavin A.C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M., Rau C., Jensen L.J., Bastuck S., Dumpelfeld B., Edelmann A., Heurtier M.A., Hoffman V., Hoefert C., Klein K., Hudak M., Michon A.M., Schelder M., Schirle M., Remor M., Rudi T., Hooper S., Bauer A., Bouwmeester T., Casari G., Drewes G., Neubauer G., Rick J.M., Kuster B., Bork P., Russell R.B., and Superti-Furga G. Proteome survey reveals modularity of the yeast cell machinery. Nature 440 (2006) 631-636
38. Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.L., Millar A., Taylor P., Bennett K., Boutilier K., Yang L., Wolting C., Donaldson I., Schandorff S., Shewnarane J., Vo M., Taggart J., Goudreault M., Muskat B., Alfarano C., Dewar D., Lin Z., Michalickova K., Willems A.R., Sassi H., Nielsen P.A., Rasmussen K.J., Andersen J.R., Johansen L.E., Hansen L.H., Jespersen H., Podtelejnikov A., Nielsen E., Crawford J., Poulsen V., Sorensen B.D., Matthiesen J., Hendrickson R.C., Gleeson F., Pawson T., Moran M.F., Durocher D., Mann M., Hogue C.W., Figeys D., and Tyers M. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415 (2002) 180-183
39. Colwill K., Field D., Moore L., Friesen J., and Andrews B. In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions. Genetics 152 (1999) 881-893
40. Rodal A.A., Manning A.L., Goode B.L., and Drubin D.G. Negative regulation of yeast WASp by two SH3 domain-containing proteins. Curr. Biol. 13 (2003) 1000-1008
41. Imai K., Nonoyama S., and Ochs H.D. WASP (Wiskott-Aldrich syndrome protein) gene mutations and phenotype. Curr. Opin. Allergy Clin. Immunol. 3 (2003) 427-436
42. Naqvi S.N., Zahn R., Mitchell D.A., Stevenson B.J., and Munn A.L. The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast. Curr. Biol. 8 (1998) 959-962
43. Vaduva G., Martinez-Quiles N., Anton I.M., Martin N.C., Geha R.S., Hopper A.K., and Ramesh N. The human WASP-interacting protein, WIP, activates the cell polarity pathway in yeast. J. Biol. Chem. 274 (1999) 17103-17108
44. Evangelista M., Klebl B.M., Tong A.H., Webb B.A., Leeuw T., Leberer E., Whiteway M., Thomas D.Y., and Boone C. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J. Cell Biol. 148 (2000) 353-362
45. Soulard A., Lechler T., Spiridonov V., Shevchenko A., Shevchenko A., Li R., and Winsor B. Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro. Mol. Cell. Biol. 22 (2002) 7889-7906
46. Drees B.L., Sundin B., Brazeau E., Caviston J.P., Chen G.C., Guo W., Kozminski K.G., Lau M.W., Moskow J.J., Tong A., Schenkman L.R., McKenzie III A., Brennwald P., Longtine M., Bi E., Chan C., Novick P., Boone C., Pringle J.R., Davis T.N., Fields S., and Drubin D.G. A protein interaction map for cell polarity development. J. Cell Biol. 154 (2001) 549-571
47. Sun Y., Martin A.C., and Drubin D.G. Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity. Dev. Cell 11 (2006) 33-46
48. Friesen H., Murphy K., Breitkreutz A., Tyers M., and Andrews B. Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation. Mol. Biol. Cell 14 (2003) 3027-3040
49. Friesen H., Humphries C., Ho Y., Schub O., Colwill K., and Andrews B. Characterization of the yeast amphiphysins Rvs161p and Rvs167p reveals roles for the Rvs heterodimer in vivo. Mol. Biol. Cell 17 (2006) 1306-1321