Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1843, Issue 1, 2014, Pages 61-74

  Scheffner, Martin ^a   Kumar, Sharad ^b,c,d  

^a UNIVERSITY OF KONSTANZ   (Germany)

^b CENTRE FOR CANCER BIOLOGY   (Australia)

^c UNIVERSITY OF ADELAIDE   (Australia)

^d UNIVERSITY OF SOUTH AUSTRALIA   (Australia)

Author keywords

Disease; HECT domain; Signaling; Ubiquitin ligase; Ubiquitination

Indexed keywords

EPITHELIAL SODIUM CHANNEL; HERC1 PROTEIN; HERC2 PROTEIN; SMURF1 PROTEIN; SMURF2 PROTEIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG; WWP1 PROTEIN; WWP2 PROTEIN;

ALLERGIC REACTION; AMINO TERMINAL SEQUENCE; ARTICLE; BIOLOGICAL FUNCTIONS; CARBOXY TERMINAL SEQUENCE; CARCINOGENESIS; CARDIOVASCULAR DISEASE; CHROMOSOME REARRANGEMENT; DEREGULATION; DNA REPAIR; GENE LOCATION; GENE LOCUS; HUMAN; IMMUNE RESPONSE; MAMMAL CELL; MITOGENESIS; NEUROLOGIC DISEASE; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; SURVIVAL; TUMOR CELL; UBIQUITINATION; UTERINE CERVIX CANCER; VIRUS INFECTION;

MAMMALIA;

EID: 84890136771     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.03.024     Document Type: Article

References (258)

1. Kerscher O., Felberbaum R., Hochstrasser M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu. Rev. Cell Dev. Biol. 2006, 22:159-180.
2. Varshavsky A. The ubiquitin system, an immense realm. Annu. Rev. Biochem. 2012, 81:167-176.
3. Metzger M.B., Hristova V.A., Weissman A.M. HECT and RING finger families of E3 ubiquitin ligases at a glance. J. Cell Sci. 2012, 125:531-537.
4. Scheffner M., Staub O. HECT E3s and human disease. BMC Biochem. 2007, 8(Suppl. 1):S6.
5. Rotin D., Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2009, 10:398-409.
6. Deshaies R.J., Joazeiro C.A. RING domain E3 ubiquitin ligases. Annu. Rev. Biochem. 2009, 78:399-434.
7. Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 2012, 474:105-108.
8. Smit J.J., Monteferrario D., Noordermeer S.M., van Dijk W.J., van der Reijden B.A., Sixma T.K. The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension. EMBO J. 2012, 31:3833-3844.
9. Stieglitz B., Morris-Davies A.C., Koliopoulos M.G., Christodoulou E., Rittinger K. LUBAC synthesizes linear ubiquitin chains via a thioester intermediate. EMBO Rep. 2012, 13:840-846.
10. Wenzel D.M., Klevit R.E. Following Ariadne's thread: a new perspective on RBR ubiquitin ligases. BMC Biol. 2012, 10:24.
11. Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:2563-2567.
12. Lin D.Y., Diao J., Chen J. Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:1925-1930.
13. Lin D.Y., Diao J., Zhou D., Chen J. Biochemical and structural studies of a HECT-like ubiquitin ligase from Escherichia coli O157:H7. J. Biol. Chem. 2011, 286:441-449.
14. Zhang Y., Higashide W.M., McCormick B.A., Chen J., Zhou D. The inflammation-associated Salmonella SopA is a HECT-like E3 ubiquitin ligase. Mol. Microbiol. 2006, 62:786-793.
15. Diao J., Zhang Y., Huibregtse J.M., Zhou D., Chen J. Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase. Nat. Struct. Mol. Biol. 2008, 15:65-70.
16. Scheffner M., Nuber U., Huibregtse J.M. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 1995, 373:81-83.
17. Marin I. Animal HECT ubiquitin ligases: evolution and functional implications. BMC Evol. Biol. 2010, 10:56.
18. Kar G., Keskin O., Nussinov R., Gursoy A. Human proteome-scale structural modeling of E2-E3 interactions exploiting interface motifs. J. Proteome Res. 2012, 11:1196-1207.
19. Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H., Raught B., Dhe-Paganon S. A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen. Mol. Cell. Proteomics 2012, 11:329-341.
20. Schwarz S.E., Rosa J.L., Scheffner M. Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J. Biol. Chem. 1998, 273:12148-12154.
21. Huang L., Kinnucan E., Wang G., Beaudenon S., Howley P.M., Huibregtse J.M., Pavletich N.P. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 1999, 286:1321-1326.
22. Verdecia M.A., Joazeiro C.A., Wells N.J., Ferrer J.L., Bowman M.E., Hunter T., Noel J.P. Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol. Cell 2003, 11:249-259.
23. Ogunjimi A.A., Briant D.J., Pece-Barbara N., Le Roy C., Di Guglielmo G.M., Kavsak P., Rasmussen R.K., Seet B.T., Sicheri F., Wrana J.L. Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain. Mol. Cell 2005, 19:297-308.
24. Kamadurai H.B., Souphron J., Scott D.C., Duda D.M., Miller D.J., Stringer D., Piper R.C., Schulman B.A. Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex. Mol. Cell 2009, 36:1095-1102.
25. Pandya R.K., Partridge J.R., Love K.R., Schwartz T.U., Ploegh H.L. A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities. J. Biol. Chem. 2010, 285:5664-5673.
26. Kim H.C., Steffen A.M., Oldham M.L., Chen J., Huibregtse J.M. Structure and function of a HECT domain ubiquitin-binding site. EMBO Rep. 2011, 12:334-341.
27. Maspero E., Mari S., Valentini E., Musacchio A., Fish A., Pasqualato S., Polo S. Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation. EMBO Rep. 2011, 12:342-349.
28. Matta-Camacho E., Kozlov G., Menade M., Gehring K. Structure of the HECT C-lobe of the UBR5 E3 ubiquitin ligase. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2012, 68:1158-1163.
29. Harvey K.F., Shearwin-Whyatt L.M., Fotia A., Parton R.G., Kumar S. N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein. J. Biol. Chem. 2002, 277:9307-9317.
30. Shearwin-Whyatt L., Dalton H.E., Foot N., Kumar S. Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins. Bioessays 2006, 28:617-628.
31. Shearwin-Whyatt L.M., Brown D.L., Wylie F.G., Stow J.L., Kumar S. N4WBP5A (Ndfip2), a Nedd4-interacting protein, localizes to multivesicular bodies and the Golgi, and has a potential role in protein trafficking. J. Cell Sci. 2004, 117:3679-3689.
32. Shea F.F., Rowell J.L., Li Y., Chang T.H., Alvarez C.E. Mammalian alpha arrestins link activated seven transmembrane receptors to Nedd4 family e3 ubiquitin ligases and interact with beta arrestins. PLoS One 2012, 7:e50557.
33. Han S.O., Kommaddi R.P., Shenoy S.K. Distinct roles for beta-arrestin2 and arrestin-domain-containing proteins in beta(2) adrenergic receptor trafficking. EMBO Rep. 2013, 14:164-171.
34. Bhalla V., Daidie D., Li H., Pao A.C., LaGrange L.P., Wang J., Vandewalle A., Stockand J.D., Staub O., Pearce D. Serum- and glucocorticoid-regulated kinase 1 regulates ubiquitin ligase neural precursor cell-expressed, developmentally down-regulated protein 4-2 by inducing interaction with 14-3-3. Mol. Endocrinol. 2005, 19:3073-3084.
35. Ichimura T., Yamamura H., Sasamoto K., Tominaga Y., Taoka M., Kakiuchi K., Shinkawa T., Takahashi N., Shimada S., Isobe T. 14-3-3 proteins modulate the expression of epithelial Na+ channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase. J. Biol. Chem. 2005, 280:13187-13194.
36. Lee I.H., Dinudom A., Sanchez-Perez A., Kumar S., Cook D.I. Akt mediates the effect of insulin on epithelial sodium channels by inhibiting Nedd4-2. J. Biol. Chem. 2007, 282:29866-29873.
37. Kee Y., Huibregtse J.M. Regulation of catalytic activities of HECT ubiquitin ligases. Biochem. Biophys. Res. Commun. 2007, 354:329-333.
38. Becuwe M., Herrador A., Haguenauer-Tsapis R., Vincent O., Leon S. Ubiquitin-mediated regulation of endocytosis by proteins of the arrestin family. Biochem. Res. Int. 2012, 2012:242764.
39. Polo S. Signaling-mediated control of ubiquitin ligases in endocytosis. BMC Biol. 2012, 10:25.
40. Wiesner S., Ogunjimi A.A., Wang H.R., Rotin D., Sicheri F., Wrana J.L., Forman-Kay J.D. Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain. Cell 2007, 130:651-662.
41. Gallagher E., Gao M., Liu Y.C., Karin M. Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:1717-1722.
42. Behrends C., Harper J.W. Constructing and decoding unconventional ubiquitin chains. Nat. Struct. Mol. Biol. 2011, 18:520-528.
43. Kravtsova-Ivantsiv Y., Ciechanover A. Non-canonical ubiquitin-based signals for proteasomal degradation. J. Cell Sci. 2012, 125:539-548.
44. Komander D., Rape M. The ubiquitin code. Annu. Rev. Biochem. 2012, 81:203-229.
45. Kulathu Y., Komander D. Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat. Rev. Mol. Cell Biol. 2012, 13:508-523.
46. Husnjak K., Dikic I. Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu. Rev. Biochem. 2012, 81:291-322.
47. Wang M., Pickart C.M. Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis. EMBO J. 2005, 24:4324-4333.
48. Kim H.T., Kim K.P., Lledias F., Kisselev A.F., Scaglione K.M., Skowyra D., Gygi S.P., Goldberg A.L. Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J. Biol. Chem. 2007, 282:17375-17386.
49. Scialpi F., Malatesta M., Peschiaroli A., Rossi M., Melino G., Bernassola F. Itch self-polyubiquitylation occurs through lysine-63 linkages. Biochem. Pharmacol. 2008, 76:1515-1521.
50. Kim H.C., Huibregtse J.M. Polyubiquitination by HECT E3s and the determinants of chain type specificity. Mol. Cell. Biol. 2009, 29:3307-3318.
51. Wang M., Cheng D., Peng J., Pickart C.M. Molecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase. EMBO J. 2006, 25:1710-1719.
52. Ogunjimi A.A., Wiesner S., Briant D.J., Varelas X., Sicheri F., Forman-Kay J., Wrana J.L. The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substrates. J. Biol. Chem. 2010, 285:6308-6315.
53. French M.E., Kretzmann B.R., Hicke L. Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site. J. Biol. Chem. 2009, 284:12071-12079.
54. Hwang C.S., Shemorry A., Auerbach D., Varshavsky A. The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases. Nat. Cell Biol. 2010, 12:1177-1185.
55. Kumar S., Tomooka Y., Noda M. Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem. Biophys. Res. Commun. 1992, 185:1155-1161.
56. Kumar S., Harvey K.F., Kinoshita M., Copeland N.G., Noda M., Jenkins N.A. cDNA cloning, expression analysis, and mapping of the mouse Nedd4 gene. Genomics 1997, 40:435-443.
57. Harvey K.F., Kumar S. Nedd4-like proteins: an emerging family of ubiquitin-protein ligases implicated in diverse cellular functions. Trends Cell Biol. 1999, 9:166-169.
58. Staub O., Gautschi I., Ishikawa T., Breitschopf K., Ciechanover A., Schild L., Rotin D. Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination. EMBO J. 1997, 16:6325-6336.
59. Sudol M., Hunter T. NeW wrinkles for an old domain. Cell 2000, 103:1001-1004.
60. Yang B., Kumar S. Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with distinct physiological functions. Cell Death Differ. 2010, 17:68-77.
61. Katz M., Shtiegman K., Tal-Or P., Yakir L., Mosesson Y., Harari D., Machluf Y., Asao H., Jovin T., Sugamura K., Yarden Y. Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic 2002, 3:740-751.
62. Cao X.R., Lill N.L., Boase N., Shi P.P., Croucher D.R., Shan H., Qu J., Sweezer E.M., Place T., Kirby P.A., Daly R.J., Kumar S., Yang B. Nedd4 controls animal growth by regulating IGF-1 signaling. Sci. Signal. 2008, 1:ra5.
63. Morrione A., Plant P., Valentinis B., Staub O., Kumar S., Rotin D., Baserga R. mGrb10 interacts with Nedd4. J. Biol. Chem. 1999, 274:24094-24099.
64. Huang Q., Szebenyi D.M. Structural basis for the interaction between the growth factor-binding protein GRB10 and the E3 ubiquitin ligase NEDD4. J. Biol. Chem. 2010, 285:42130-42139.
65. Yang B., Gay D.L., MacLeod M.K., Cao X., Hala T., Sweezer E.M., Kappler J., Marrack P., Oliver P.M. Nedd4 augments the adaptive immune response by promoting ubiquitin-mediated degradation of Cbl-b in activated T cells. Nat. Immunol. 2008, 9:1356-1363.
66. Kawabe H., Neeb A., Dimova K., Young S.M., Takeda M., Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E., Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O., Rhee J., Brose N. Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite development. Neuron 2010, 65:358-372.
67. Drinjakovic J., Jung H., Campbell D.S., Strochlic L., Dwivedy A., Holt C.E. E3 ligase Nedd4 promotes axon branching by downregulating PTEN. Neuron 2010, 65:341-357.
68. Liu Y., Oppenheim R.W., Sugiura Y., Lin W. Abnormal development of the neuromuscular junction in Nedd4-deficient mice. Dev. Biol. 2009, 330:153-166.
69. Nagpal P., Plant P.J., Correa J., Bain A., Takeda M., Kawabe H., Rotin D., Bain J.R., Batt J.A. The ubiquitin ligase nedd4-1 participates in denervation-induced skeletal muscle atrophy in mice. PLoS One 2012, 7:e46427.
70. Fouladkou F., Lu C., Jiang C., Zhou L., She Y., Walls J.R., Kawabe H., Brose N., Henkelman R.M., Huang A., Bruneau B.G., Rotin D. The ubiquitin ligase Nedd4-1 is required for heart development and is a suppressor of thrombospondin-1. J. Biol. Chem. 2010, 285:6770-6780.
71. Liu P.Y., Xu N., Malyukova A., Scarlett C.J., Sun Y.T., Zhang X.D., Ling D., Su S.P., Nelson C., Chang D.K., Koach J., Tee A.E., Haber M., Norris M.D., Toon C., Rooman I., Xue C., Cheung B.B., Kumar S., Marshall G.M., Biankin A.V., Liu T. The histone deacetylase SIRT2 stabilizes Myc oncoproteins. Cell Death Differ. 2013, 20:503-514.
72. Yasuda J., Nakao M., Kawaoka Y., Shida H. Nedd4 regulates egress of Ebola virus-like particles from host cells. J. Virol. 2003, 77:9987-9992.
73. Timmins J., Schoehn G., Ricard-Blum S., Scianimanico S., Vernet T., Ruigrok R.W., Weissenhorn W. Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4. J. Mol. Biol. 2003, 326:493-502.
74. Blot V., Perugi F., Gay B., Prevost M.C., Briant L., Tangy F., Abriel H., Staub O., Dokhelar M.C., Pique C. Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. J. Cell Sci. 2004, 117:2357-2367.
75. Kikonyogo A., Bouamr F., Vana M.L., Xiang Y., Aiyar A., Carter C., Leis J. Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:11199-11204.
76. Yasuda J., Hunter E., Nakao M., Shida H. Functional involvement of a novel Nedd4-like ubiquitin ligase on retrovirus budding. EMBO Rep. 2002, 3:636-640.
77. Bouamr F., Melillo J.A., Wang M.Q., Nagashima K., de Los Santos M., Rein A., Goff S.P. PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101 [corrected]. J. Virol. 2003, 77:11882-11895.
78. Vana M.L., Tang Y., Chen A., Medina G., Carter C., Leis J. Role of Nedd4 and ubiquitination of Rous sarcoma virus Gag in budding of virus-like particles from cells. J. Virol. 2004, 78:13943-13953.
79. Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., Basyuk E. Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding. J. Biol. Chem. 2005, 280:27004-27012.
80. Ikeda A., Caldwell R.G., Longnecker R., Ikeda M. Itchy, a Nedd4 ubiquitin ligase, downregulates latent membrane protein 2A activity in B-cell signaling. J. Virol. 2003, 77:5529-5534.
81. Boase N.A., Rychkov G.Y., Townley S.L., Dinudom A., Candi E., Voss A.K., Tsoutsman T., Semsarian C., Melino G., Koentgen F., Cook D.I., Kumar S. Respiratory distress and perinatal lethality in Nedd4-2-deficient mice. Nat. Commun. 2011, 2:287.
82. Kimura T., Kawabe H., Jiang C., Zhang W., Xiang Y.Y., Lu C., Salter M.W., Brose N., Lu W.Y., Rotin D. Deletion of the ubiquitin ligase Nedd4L in lung epithelia causes cystic fibrosis-like disease. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:3216-3221.
83. Harvey K.F., Dinudom A., Cook D.I., Kumar S. The Nedd4-like protein KIAA0439 is a potential regulator of the epithelial sodium channel. J. Biol. Chem. 2001, 276:8597-8601.
84. Kamynina E., Debonneville C., Bens M., Vandewalle A., Staub O. A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+ channel. FASEB J. 2001, 15:204-214.
85. Fotia A.B., Dinudom A., Shearwin K.E., Koch J.P., Korbmacher C., Cook D.I., Kumar S. The role of individual Nedd4-2 (KIAA0439) WW domains in binding and regulating epithelial sodium channels. FASEB J. 2003, 17:70-72.
86. Lifton R.P. Genetic determinants of human hypertension. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:8545-8551.
87. Shi P.P., Cao X.R., Sweezer E.M., Kinney T.S., Williams N.R., Husted R.F., Nair R., Weiss R.M., Williamson R.A., Sigmund C.D., Snyder P.M., Staub O., Stokes J.B., Yang B. Salt-sensitive hypertension and cardiac hypertrophy in mice deficient in the ubiquitin ligase Nedd4-2. Am. J. Physiol. Renal Physiol. 2008, 295:F462-F470.
88. Ronzaud C., Loffing-Cueni D., Hausel P., Debonneville A., Malsure S.R., Fowler-Jaeger N., Boase N.A., Perrier R., Maillard M., Yang B., Stokes J.B., Koesters R., Kumar S., Hummler E., Loffing J., Staub O. Renal tubular NEDD4-2 deficiency causes NCC-mediated salt-dependent hypertension. J. Clin. Invest. 2013, 123:657-665.
89. Henke G., Maier G., Wallisch S., Boehmer C., Lang F. Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1. J. Cell. Physiol. 2004, 199:194-199.
90. Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S. Regulation of neuronal voltage-gated sodium channels by the ubiquitin-protein ligases Nedd4 and Nedd4-2. J. Biol. Chem. 2004, 279:28930-28935.
91. van Bemmelen M.X., Rougier J.S., Gavillet B., Apotheloz F., Daidie D., Tateyama M., Rivolta I., Thomas M.A., Kass R.S., Staub O., Abriel H. Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination. Circ. Res. 2004, 95:284-291.
92. Rougier J.S., van Bemmelen M.X., Bruce M.C., Jespersen T., Gavillet B., Apotheloz F., Cordonier S., Staub O., Rotin D., Abriel H. Molecular determinants of voltage-gated sodium channel regulation by the Nedd4/Nedd4-like proteins. Am. J. Physiol. Cell Physiol. 2005, 288:C692-C701.
93. Ekberg J., Schuetz F., Boase N.A., Conroy S.J., Manning J., Kumar S., Poronnik P., Adams D.J. Regulation of the voltage-gated K(+) channels KCNQ2/3 and KCNQ3/5 by ubiquitination. Novel role for Nedd4-2. J. Biol. Chem. 2007, 282:12135-12142.
94. Jespersen T., Membrez M., Nicolas C.S., Pitard B., Staub O., Olesen S.P., Baro I., Abriel H. The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family. Cardiovasc. Res. 2007, 74:64-74.
95. Sorkina T., Miranda M., Dionne K.R., Hoover B.R., Zahniser N.R., Sorkin A. RNA interference screen reveals an essential role of Nedd4-2 in dopamine transporter ubiquitination and endocytosis. J. Neurosci. 2006, 26:8195-8205.
96. Van Campenhout C.A., Eitelhuber A., Gloeckner C.J., Giallonardo P., Gegg M., Oller H., Grant S.G., Krappmann D., Ueffing M., Lickert H. Dlg3 trafficking and apical tight junction formation is regulated by nedd4 and nedd4-2 e3 ubiquitin ligases. Dev. Cell 2011, 21:479-491.
97. Perry W.L., Hustad C.M., Swing D.A., O'Sullivan T.N., Jenkins N.A., Copeland N.G. The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice. Nat. Genet. 1998, 18:143-146.
98. Lohr N.J., Molleston J.P., Strauss K.A., Torres-Martinez W., Sherman E.A., Squires R.H., Rider N.L., Chikwava K.R., Cummings O.W., Morton D.H., Puffenberger E.G. Human ITCH E3 ubiquitin ligase deficiency causes syndromic multisystem autoimmune disease. Am. J. Hum. Genet. 2010, 86:447-453.
99. Gao M., Labuda T., Xia Y., Gallagher E., Fang D., Liu Y.C., Karin M. Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch. Science 2004, 306:271-275.
100. Venuprasad K. Cbl-b and itch: key regulators of peripheral T-cell tolerance. Cancer Res. 2010, 70:3009-3012.
101. Ahmed N., Zeng M., Sinha I., Polin L., Wei W.Z., Rathinam C., Flavell R., Massoumi R., Venuprasad K. The E3 ligase Itch and deubiquitinase Cyld act together to regulate Tak1 and inflammation. Nat. Immunol. 2011, 12:1176-1183.
102. Venuprasad K., Huang H., Harada Y., Elly C., Subramaniam M., Spelsberg T., Su J., Liu Y.C. The E3 ubiquitin ligase Itch regulates expression of transcription factor Foxp3 and airway inflammation by enhancing the function of transcription factor TIEG1. Nat. Immunol. 2008, 9:245-253.
103. Shembade N., Harhaj N.S., Parvatiyar K., Copeland N.G., Jenkins N.A., Matesic L.E., Harhaj E.W. The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20. Nat. Immunol. 2008, 9:254-262.
104. You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z. PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4. Nat. Immunol. 2009, 10:1300-1308.
105. Rathinam C., Matesic L.E., Flavell R.A. The E3 ligase Itch is a negative regulator of the homeostasis and function of hematopoietic stem cells. Nat. Immunol. 2011, 12:399-407.
106. Mossinger J., Wieffer M., Krause E., Freund C., Gerth F., Krauss M., Haucke V. Phosphatidylinositol 4-kinase IIalpha function at endosomes is regulated by the ubiquitin ligase Itch. EMBO Rep. 2012, 13:1087-1094.
107. Rossi M., De Laurenzi V., Munarriz E., Green D.R., Liu Y.C., Vousden K.H., Cesareni G., Melino G. The ubiquitin-protein ligase Itch regulates p73 stability. EMBO J. 2005, 24:836-848.
108. Rossi M., Aqeilan R.I., Neale M., Candi E., Salomoni P., Knight R.A., Croce C.M., Melino G. The E3 ubiquitin ligase Itch controls the protein stability of p63. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:12753-12758.
109. Marchese A., Raiborg C., Santini F., Keen J.H., Stenmark H., Benovic J.L. The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4. Dev. Cell 2003, 5:709-722.
110. Chang L., Kamata H., Solinas G., Luo J.L., Maeda S., Venuprasad K., Liu Y.C., Karin M. The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover. Cell 2006, 124:601-613.
111. Carrano A.C., Liu Z., Dillin A., Hunter T. A conserved ubiquitination pathway determines longevity in response to diet restriction. Nature 2009, 460:396-399.
112. Zhi X., Chen C. WWP1: a versatile ubiquitin E3 ligase in signaling and diseases. Cell. Mol. Life Sci. 2012, 69:1425-1434.
113. Subik K., Shu L., Wu C., Liang Q., Hicks D., Boyce B., Schiffhauer L., Chen D., Chen C., Tang P., Xing L. The ubiquitin E3 ligase WWP1 decreases CXCL12-mediated MDA231 breast cancer cell migration and bone metastasis. Bone 2012, 50:813-823.
114. Zhao L., Huang J., Zhang H., Wang Y., Matesic L.E., Takahata M., Awad H., Chen D., Xing L. Tumor necrosis factor inhibits mesenchymal stem cell differentiation into osteoblasts via the ubiquitin E3 ligase Wwp1. Stem Cells 2011, 29:1601-1610.
115. Foot N.J., Dalton H.E., Shearwin-Whyatt L.M., Dorstyn L., Tan S.S., Yang B., Kumar S. Regulation of the divalent metal ion transporter DMT1 and iron homeostasis by a ubiquitin-dependent mechanism involving Ndfips and WWP2. Blood 2008, 112:4268-4275.
116. Foot N.J., Leong Y.A., Dorstyn L.E., Dalton H.E., Ho K., Zhao L., Garrick M.D., Yang B., Hiwase D., Kumar S. Ndfip1-deficient mice have impaired DMT1 regulation and iron homeostasis. Blood 2011, 117:638-646.
117. Zou W., Chen X., Shim J.H., Huang Z., Brady N., Hu D., Drapp R., Sigrist K., Glimcher L.H., Jones D. The E3 ubiquitin ligase Wwp2 regulates craniofacial development through mono-ubiquitylation of Goosecoid. Nat. Cell Biol. 2011, 13:59-65.
118. Maddika S., Kavela S., Rani N., Palicharla V.R., Pokorny J.L., Sarkaria J.N., Chen J. WWP2 is an E3 ubiquitin ligase for PTEN. Nat. Cell Biol. 2011, 13:728-733.
119. Howitt J., Putz U., Lackovic J., Doan A., Dorstyn L., Cheng H., Yang B., Chan-Ling T., Silke J., Kumar S., Tan S.S. Divalent metal transporter 1 (DMT1) regulation by Ndfip1 prevents metal toxicity in human neurons. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:15489-15494.
120. Xu H.M., Liao B., Zhang Q.J., Wang B.B., Li H., Zhong X.M., Sheng H.Z., Zhao Y.X., Zhao Y.M., Jin Y. Wwp2, an E3 ubiquitin ligase that targets transcription factor Oct-4 for ubiquitination. J. Biol. Chem. 2004, 279:23495-23503.
121. Xu H., Wang W., Li C., Yu H., Yang A., Wang B., Jin Y. WWP2 promotes degradation of transcription factor OCT4 in human embryonic stem cells. Cell Res. 2009, 19:561-573.
122. Nakamura Y., Yamamoto K., He X., Otsuki B., Kim Y., Murao H., Soeda T., Tsumaki N., Deng J.M., Zhang Z., Behringer R.R., Crombrugghe B., Postlethwait J.H., Warman M.L., Nakamura T., Akiyama H. Wwp2 is essential for palatogenesis mediated by the interaction between Sox9 and mediator subunit 25. Nat. Commun. 2011, 2:251.
123. 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., Jiang X. NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell 2007, 128:129-139.
124. Trotman L.C., Wang X., Alimonti A., Chen Z., Teruya-Feldstein J., Yang H., Pavletich N.P., Carver B.S., Cordon-Cardo C., Erdjument-Bromage H., Tempst P., Chi S.G., Kim H.J., Misteli T., Jiang X., Pandolfi P.P. Ubiquitination regulates PTEN nuclear import and tumor suppression. Cell 2007, 128:141-156.
125. Fouladkou F., Landry T., Kawabe H., Neeb A., Lu C., Brose N., Stambolic V., Rotin D. The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localization. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:8585-8590.
126. Howitt J., Lackovic J., Low L.H., Naguib A., Macintyre A., Goh C.P., Callaway J.K., Hammond V., Thomas T., Dixon M., Putz U., Silke J., Bartlett P., Yang B., Kumar S., Trotman L.C., Tan S.S. Ndfip1 regulates nuclear Pten import in vivo to promote neuronal survival following cerebral ischemia. J. Cell Biol. 2012, 196:29-36.
127. David D., Nair S.A., Pillai M.R. Smurf E3 ubiquitin ligases at the cross roads of oncogenesis and tumor suppression. Biochim. Biophys. Acta 2013, 1835:119-128.
128. Massague J. TGF-beta signal transduction. Annu. Rev. Biochem. 1998, 67:753-791.
129. Attisano L., Wrana J.L. Signal transduction by the TGF-beta superfamily. Science 2002, 296:1646-1647.
130. Heldin C.H., Miyazono K., ten Dijke P. TGF-beta signalling from cell membrane to nucleus through SMAD proteins. Nature 1997, 390:465-471.
131. Yamashita M., Ying S.X., Zhang G.M., Li C., Cheng S.Y., Deng C.X., Zhang Y.E. Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation. Cell 2005, 121:101-113.
132. Narimatsu M., Bose R., Pye M., Zhang L., Miller B., Ching P., Sakuma R., Luga V., Roncari L., Attisano L., Wrana J.L. Regulation of planar cell polarity by Smurf ubiquitin ligases. Cell 2009, 137:295-307.
133. Tang L.Y., Yamashita M., Coussens N.P., Tang Y., Wang X., Li C., Deng C.X., Cheng S.Y., Zhang Y.E. Ablation of Smurf2 reveals an inhibition in TGF-beta signalling through multiple mono-ubiquitination of Smad3. EMBO J. 2011, 30:4777-4789.
134. Ramkumar C., Kong Y., Cui H., Hao S., Jones S.N., Gerstein R.M., Zhang H. Smurf2 regulates the senescence response and suppresses tumorigenesis in mice. Cancer Res. 2012, 72:2714-2719.
135. Blank M., Tang Y., Yamashita M., Burkett S.S., Cheng S.Y., Zhang Y.E. A tumor suppressor function of Smurf2 associated with controlling chromatin landscape and genome stability through RNF20. Nat. Med. 2012, 18:227-234.
136. Wang T. The 26S proteasome system in the signaling pathways of TGF-beta superfamily. Front. Biosci. 2003, 8:d1109-d1127.
137. Miyazaki K., Fujita T., Ozaki T., Kato C., Kurose Y., Sakamoto M., Kato S., Goto T., Itoyama Y., Aoki M., Nakagawara A. NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1, targets mutant superoxide dismutase-1. J. Biol. Chem. 2004, 279:11327-11335.
138. Zhang L., Haraguchi S., Koda T., Hashimoto K., Nakagawara A. Muscle atrophy and motor neuron degeneration in human NEDL1 transgenic mice. J. Biomed. Biotechnol. 2011, 2011:831092.
139. Li Y., Ozaki T., Kikuchi H., Yamamoto H., Ohira M., Nakagawara A. A novel HECT-type E3 ubiquitin protein ligase NEDL1 enhances the p53-mediated apoptotic cell death in its catalytic activity-independent manner. Oncogene 2008, 27:3700-3709.
140. Shinada K., Tsukiyama T., Sho T., Okumura F., Asaka M., Hatakeyama S. RNF43 interacts with NEDL1 and regulates p53-mediated transcription. Biochem. Biophys. Res. Commun. 2011, 404:143-147.
141. Li Y., Zhou Z., Alimandi M., Chen C. WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer. Oncogene 2009, 28:2948-2958.
142. Miyazaki K., Ozaki T., Kato C., Hanamoto T., Fujita T., Irino S., Watanabe K., Nakagawa T., Nakagawara A. A novel HECT-type E3 ubiquitin ligase, NEDL2, stabilizes p73 and enhances its transcriptional activity. Biochem. Biophys. Res. Commun. 2003, 308:106-113.
143. Garcia-Gonzalo F.R., Rosa J.L. The HERC proteins: functional and evolutionary insights. Cell. Mol. Life Sci. 2005, 62:1826-1838.
144. Hochrainer K., Mayer H., Baranyi U., Binder B., Lipp J., Kroismayr R. The human HERC family of ubiquitin ligases: novel members, genomic organization, expression profiling, and evolutionary aspects. Genomics 2005, 85:153-164.
145. Bischoff F.R., Ponstingl H. Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature 1991, 354:80-82.
146. Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M., Wittinghofer A. The 1.7 A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature 1998, 392:97-101.
147. Renault L., Kuhlmann J., Henkel A., Wittinghofer A. Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation. Cell 2001, 105:245-255.
148. Nemergut M.E., Mizzen C.A., Stukenberg T., Allis C.D., Macara I.G. Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B. Science 2001, 292:1540-1543.
149. Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M. p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins. EMBO J. 1996, 15:4262-4273.
150. Chong-Kopera H., Inoki K., Li Y., Zhu T., Garcia-Gonzalo F.R., Rosa J.L., Guan K.L. TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase. J. Biol. Chem. 2006, 281:8313-8316.
151. Diouf B., Cheng Q., Krynetskaia N.F., Yang W., Cheok M., Pei D., Fan Y., Cheng C., Krynetskiy E.Y., Geng H., Chen S., Thierfelder W.E., Mullighan C.G., Downing J.R., Hsieh P., Pui C.H., Relling M.V., Evans W.E. Somatic deletions of genes regulating MSH2 protein stability cause DNA mismatch repair deficiency and drug resistance in human leukemia cells. Nat. Med. 2011, 17:1298-1303.
152. Mashimo T., Hadjebi O., Amair-Pinedo F., Tsurumi T., Langa F., Serikawa T., Sotelo C., Guenet J.L., Rosa J.L. Progressive Purkinje cell degeneration in tambaleante mutant mice is a consequence of a missense mutation in HERC1 E3 ubiquitin ligase. PLoS Genet. 2009, 5:e1000784.
153. Lehman A.L., Nakatsu Y., Ching A., Bronson R.T., Oakey R.J., Keiper-Hrynko N., Finger J.N., Durham-Pierre D., Horton D.B., Newton J.M., Lyon M.F., Brilliant M.H. A very large protein with diverse functional motifs is deficient in rjs (runty, jerky, sterile) mice. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:9436-9441.
154. Walkowicz M., Ji Y., Ren X., Horsthemke B., Russell L.B., Johnson D., Rinchik E.M., Nicholls R.D., Stubbs L. Molecular characterization of radiation- and chemically induced mutations associated with neuromuscular tremors, runting, juvenile lethality, and sperm defects in jdf2 mice. Mamm. Genome 1999, 10:870-878.
155. Bekker-Jensen S., Rendtlew Danielsen J., Fugger K., Gromova I., Nerstedt A., Lukas C., Bartek J., Lukas J., Mailand N. HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Nat. Cell Biol. 2010, 12:80-86. (sup pp 81-12).
156. Kang T.H., Reardon J.T., Sancar A. Regulation of nucleotide excision repair activity by transcriptional and post-transcriptional control of the XPA protein. Nucleic Acids Res. 2010, 39:3176-3187.
157. Wu W., Sato K., Koike A., Nishikawa H., Koizumi H., Venkitaraman A.R., Ohta T. HERC2 is an E3 ligase that targets BRCA1 for degradation. Cancer Res. 2010, 70:6384-6392.
158. Danielsen J.R., Povlsen L.K., Villumsen B.H., Streicher W., Nilsson J., Wikstrom M., Bekker-Jensen S., Mailand N. DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger. J. Cell Biol. 2012, 197:179-187.
159. Oestergaard V.H., Pentzold C., Pedersen R.T., Iosif S., Alpi A., Bekker-Jensen S., Mailand N., Lisby M. RNF8 and RNF168 but not HERC2 are required for DNA damage-induced ubiquitylation in chicken DT40 cells. DNA Repair (Amst) 2012, 11:892-905.
160. Izawa N., Wu W., Sato K., Nishikawa H., Kato A., Boku N., Itoh F., Ohta T. HERC2 Interacts with Claspin and regulates DNA origin firing and replication fork progression. Cancer Res. 2011, 71:5621-5625.
161. Nicholls R.D., Knepper J.L. Genome organization, function, and imprinting in Prader-Willi and Angelman syndromes. Annu. Rev. Genomics Hum. Genet. 2001, 2:153-175.
162. Chamberlain S.J., Lalande M. Neurodevelopmental disorders involving genomic imprinting at human chromosome 15q11-q13. Neurobiol. Dis. 2010, 39:13-20.
163. Puffenberger E.G., Jinks R.N., Wang H., Xin B., Fiorentini C., Sherman E.A., Degrazio D., Shaw C., Sougnez C., Cibulskis K., Gabriel S., Kelley R.I., Morton D.H., Strauss K.A. A homozygous missense mutation in HERC2 associated with global developmental delay and autism spectrum disorder. Hum. Mutat. 2012, 33:1639-1646.
164. Harlalka G.V., Baple E.L., Cross H., Kuhnle S., Cubillos-Rojas M., Matentzoglu K., Patton M.A., Wagner K., Coblentz R., Ford D.L., Mackay D.J., Chioza B.A., Scheffner M., Rosa J.L., Crosby A.H. Mutation of HERC2 causes developmental delay with Angelman-like features. J. Med. Genet. 2013, 50:65-73.
165. Kuhnle S., Kogel U., Glockzin S., Marquardt A., Ciechanover A., Matentzoglu K., Scheffner M. Physical and functional interaction of the HECT ubiquitin-protein ligases E6AP and HERC2. J. Biol. Chem. 2011, 286:19410-19416.
166. Dagli A., Buiting K., Williams C.A. Molecular and clinical aspects of Angelman syndrome. Mol. Syndromol. 2012, 2:100-112.
167. Clayton-Smith J., Laan L. Angelman syndrome: a review of the clinical and genetic aspects. J. Med. Genet. 2003, 40:87-95.
168. Sturm R.A., Larsson M. Genetics of human iris colour and patterns. Pigment Cell Melanoma Res. 2009, 22:544-562.
169. White D., Rabago-Smith M. Genotype-phenotype associations and human eye color. J. Hum. Genet. 2011, 56:5-7.
170. Cruz C., Ventura F., Bartrons R., Rosa J.L. HERC3 binding to and regulation by ubiquitin. FEBS Lett. 2001, 488:74-80.
171. Hochrainer K., Kroismayr R., Baranyi U., Binder B.R., Lipp J. Highly homologous HERC proteins localize to endosomes and exhibit specific interactions with hPLIC and Nm23B. Cell. Mol. Life Sci. 2008, 65:2105-2117.
172. Mitsui K., Nakanishi M., Ohtsuka S., Norwood T.H., Okabayashi K., Miyamoto C., Tanaka K., Yoshimura A., Ohtsubo M. A novel human gene encoding HECT domain and RCC1-like repeats interacts with cyclins and is potentially regulated by the tumor suppressor proteins. Biochem. Biophys. Res. Commun. 1999, 266:115-122.
173. Kroismayr R., Baranyi U., Stehlik C., Dorfleutner A., Binder B.R., Lipp J. HERC5, a HECT E3 ubiquitin ligase tightly regulated in LPS activated endothelial cells. J. Cell Sci. 2004, 117:4749-4756.
174. Dastur A., Beaudenon S., Kelley M., Krug R.M., Huibregtse J.M. Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells. J. Biol. Chem. 2006, 281:4334-4338.
175. Wong J.J., Pung Y.F., Sze N.S., Chin K.C. HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:10735-10740.
176. Jeon Y.J., Yoo H.M., Chung C.H. ISG15 and immune diseases. Biochim. Biophys. Acta 2010, 1802:485-496.
177. Oudshoorn D., van Boheemen S., Sanchez-Aparicio M.T., Rajsbaum R., Garcia-Sastre A., Versteeg G.A. HERC6 is the main E3 ligase for global ISG15 conjugation in mouse cells. PLoS One 2012, 7:e29870.
178. Ketscher L., Basters A., Prinz M., Knobeloch K.P. mHERC6 is the essential ISG15 E3 ligase in the murine system. Biochem. Biophys. Res. Commun. 2012, 417:135-140.
179. Zhao C., Hsiang T.Y., Kuo R.L., Krug R.M. ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:2253-2258.
180. Tang Y., Zhong G., Zhu L., Liu X., Shan Y., Feng H., Bu Z., Chen H., Wang C. Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein. J. Immunol. 2010, 184:5777-5790.
181. Durfee L.A., Lyon N., Seo K., Huibregtse J.M. The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15. Mol. Cell 2010, 38:722-732.
182. Beaudenon S., Huibregtse J.M. HPV E6, E6AP and cervical cancer. BMC Biochem. 2008, 9(Suppl. 1):S4.
183. Kishino T., Lalande M., Wagstaff J. UBE3A/E6-AP mutations cause Angelman syndrome. Nat. Genet. 1997, 15:70-73.
184. Matsuura T., Sutcliffe J.S., Fang P., Galjaard R.J., Jiang Y.H., Benton C.S., Rommens J.M., Beaudet A.L. De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome. Nat. Genet. 1997, 15:74-77.
185. Glessner J.T., Wang K., Cai G., Korvatska O., Kim C.E., Wood S., Zhang H., Estes A., Brune C.W., Bradfield J.P., Imielinski M., Frackelton E.C., Reichert J., Crawford E.L., Munson J., Sleiman P.M., Chiavacci R., Annaiah K., Thomas K., Hou C., Glaberson W., Flory J., Otieno F., Garris M., Soorya L., Klei L., Piven J., Meyer K.J., Anagnostou E., Sakurai T., Game R.M., Rudd D.S., Zurawiecki D., McDougle C.J., Davis L.K., Miller J., Posey D.J., Michaels S., Kolevzon A., Silverman J.M., Bernier R., Levy S.E., Schultz R.T., Dawson G., Owley T., McMahon W.M., Wassink T.H., Sweeney J.A., Nurnberger J.I., Coon H., Sutcliffe J.S., Minshew N.J., Grant S.F., Bucan M., Cook E.H., Buxbaum J.D., Devlin B., Schellenberg G.D., Hakonarson H. Autism genome-wide copy number variation reveals ubiquitin and neuronal genes. Nature 2009, 459:569-573.
186. Hogart A., Wu D., LaSalle J.M., Schanen N.C. The comorbidity of autism with the genomic disorders of chromosome 15q11.2-q13. Neurobiol. Dis. 2010, 38:181-191.
187. Huibregtse J.M., Scheffner M., Howley P.M. Cloning and expression of the cDNA for E6-AP, a protein that mediates the interaction of the human papillomavirus E6 oncoprotein with p53. Mol. Cell. Biol. 1993, 13:775-784.
188. Shai A., Pitot H.C., Lambert P.F. E6-associated protein is required for human papillomavirus type 16 E6 to cause cervical cancer in mice. Cancer Res. 2010, 70:5064-5073.
189. Scheffner M., Whitaker N.J. Human papillomavirus-induced carcinogenesis and the ubiquitin-proteasome system. Semin. Cancer Biol. 2003, 13:59-67.
190. Mantovani F., Banks L. The human papillomavirus E6 protein and its contribution to malignant progression. Oncogene 2001, 20:7874-7887.
191. Scheffner M., Huibregtse J.M., Vierstra R.D., Howley P.M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 1993, 75:495-505.
192. Malzac P., Webber H., Moncla A., Graham J.M., Kukolich M., Williams C., Pagon R.A., Ramsdell L.A., Kishino T., Wagstaff J. Mutation analysis of UBE3A in Angelman syndrome patients. Am. J. Hum. Genet. 1998, 62:1353-1360.
193. Fang P., Lev-Lehman E., Tsai T.F., Matsuura T., Benton C.S., Sutcliffe J.S., Christian S.L., Kubota T., Halley D.J., Meijers-Heijboer H., Langlois S., Graham J.M., Beuten J., Willems P.J., Ledbetter D.H., Beaudet A.L. The spectrum of mutations in UBE3A causing Angelman syndrome. Hum. Mol. Genet. 1999, 8:129-135.
194. Albrecht U., Sutcliffe J.S., Cattanach B.M., Beechey C.V., Armstrong D., Eichele G., Beaudet A.L. Imprinted expression of the murine Angelman syndrome gene, Ube3a, in hippocampal and Purkinje neurons. Nat. Genet. 1997, 17:75-78.
195. Cooper E.M., Hudson A.W., Amos J., Wagstaff J., Howley P.M. Biochemical analysis of Angelman syndrome-associated mutations in the E3 ubiquitin ligase E6-associated protein. J. Biol. Chem. 2004, 279:41208-41217.
196. Kumar S., Talis A.L., Howley P.M. Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination. J. Biol. Chem. 1999, 274:18785-18792.
197. Mani A., Oh A.S., Bowden E.T., Lahusen T., Lorick K.L., Weissman A.M., Schlegel R., Wellstein A., Riegel A.T. E6AP mediates regulated proteasomal degradation of the nuclear receptor coactivator amplified in breast cancer 1 in immortalized cells. Cancer Res. 2006, 66:8680-8686.
198. Louria-Hayon I., Alsheich-Bartok O., Levav-Cohen Y., Silberman I., Berger M., Grossman T., Matentzoglu K., Jiang Y.H., Muller S., Scheffner M., Haupt S., Haupt Y. E6AP promotes the degradation of the PML tumor suppressor. Cell Death Differ. 2009, 16:1156-1166.
199. Mulherkar S.A., Sharma J., Jana N.R. The ubiquitin ligase E6-AP promotes degradation of alpha-synuclein. J. Neurochem. 2009, 110:1955-1964.
200. Zaaroor-Regev D., de Bie P., Scheffner M., Noy T., Shemer R., Heled M., Stein I., Pikarsky E., Ciechanover A. Regulation of the polycomb protein Ring1B by self-ubiquitination or by E6-AP may have implications to the pathogenesis of Angelman syndrome. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:6788-6793.
201. Greer P.L., Hanayama R., Bloodgood B.L., Mardinly A.R., Lipton D.M., Flavell S.W., Kim T.K., Griffith E.C., Waldon Z., Maehr R., Ploegh H.L., Chowdhury S., Worley P.F., Steen J., Greenberg M.E. The Angelman Syndrome protein Ube3A regulates synapse development by ubiquitinating arc. Cell 2010, 140:704-716.
202. Jiang Y.H., Armstrong D., Albrecht U., Atkins C.M., Noebels J.L., Eichele G., Sweatt J.D., Beaudet A.L. Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation. Neuron 1998, 21:799-811.
203. Miura K., Kishino T., Li E., Webber H., Dikkes P., Holmes G.L., Wagstaff J. Neurobehavioral and electroencephalographic abnormalities in Ube3a maternal-deficient mice. Neurobiol. Dis. 2002, 9:149-159.
204. Yashiro K., Riday T.T., Condon K.H., Roberts A.C., Bernardo D.R., Prakash R., Weinberg R.J., Ehlers M.D., Philpot B.D. Ube3a is required for experience-dependent maturation of the neocortex. Nat. Neurosci. 2009, 12:777-783.
205. Tzingounis A.V., Nicoll R.A. Arc/Arg3.1: linking gene expression to synaptic plasticity and memory. Neuron 2006, 52:403-407.
206. Shepherd J.D., Bear M.F. New views of Arc, a master regulator of synaptic plasticity. Nat. Neurosci. 2011, 14:279-284.
207. Smith S.E., Zhou Y.D., Zhang G., Jin Z., Stoppel D.C., Anderson M.P. Increased gene dosage of Ube3a results in autism traits and decreased glutamate synaptic transmission in mice. Sci. Transl. Med. 2011, 3:103ra197.
208. Salvat C., Wang G., Dastur A., Lyon N., Huibregtse J.M. The -4 phenylalanine is required for substrate ubiquitination catalyzed by HECT ubiquitin ligases. J. Biol. Chem. 2004, 279:18935-18943.
209. Nawaz Z., Lonard D.M., Smith C.L., Lev-Lehman E., Tsai S.Y., Tsai M.J., O'Malley B.W. The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily. Mol. Cell. Biol. 1999, 19:1182-1189.
210. Ramamoorthy S., Nawaz Z. E6-associated protein (E6-AP) is a dual function coactivator of steroid hormone receptors. Nucl. Recept. Signal. 2008, 6:e006.
211. Gu J., Dubner R., Fornace A.J., Iadarola M.J. UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53 transactivation. Oncogene 1995, 11:2175-2178.
212. Chen D., Kon N., Li M., Zhang W., Qin J., Gu W. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 2005, 121:1071-1083.
213. Zhong Q., Gao W., Du F., Wang X. Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 2005, 121:1085-1095.
214. Liu Z., Oughtred R., Wing S.S. Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones. Mol. Cell. Biol. 2005, 25:2819-2831.
215. Adhikary S., Marinoni F., Hock A., Hulleman E., Popov N., Beier R., Bernard S., Quarto M., Capra M., Goettig S., Kogel U., Scheffner M., Helin K., Eilers M. The ubiquitin ligase HectH9 regulates transcriptional activation by Myc and is essential for tumor cell proliferation. Cell 2005, 123:409-421.
216. Zhao X., Heng J.I., Guardavaccaro D., Jiang R., Pagano M., Guillemot F., Iavarone A., Lasorella A. The HECT-domain ubiquitin ligase Huwe1 controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein. Nat. Cell Biol. 2008, 10:643-653.
217. Hall J.R., Kow E., Nevis K.R., Lu C.K., Luce K.S., Zhong Q., Cook J.G. Cdc6 stability is regulated by the Huwe1 ubiquitin ligase after DNA damage. Mol. Biol. Cell 2007, 18:3340-3350.
218. Herold S., Hock A., Herkert B., Berns K., Mullenders J., Beijersbergen R., Bernards R., Eilers M. Miz1 and HectH9 regulate the stability of the checkpoint protein, TopBP1. EMBO J. 2008, 27:2851-2861.
219. Yang Y., Do H., Tian X., Zhang C., Liu X., Dada L.A., Sznajder J.I., Liu J. E3 ubiquitin ligase Mule ubiquitinates Miz1 and is required for TNFalpha-induced JNK activation. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:13444-13449.
220. Yin L., Joshi S., Wu N., Tong X., Lazar M.A. E3 ligases Arf-bp1 and Pam mediate lithium-stimulated degradation of the circadian heme receptor Rev-erb alpha. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:11614-11619.
221. Zhang J., Kan S., Huang B., Hao Z., Mak T.W., Zhong Q. Mule determines the apoptotic response to HDAC inhibitors by targeted ubiquitination and destruction of HDAC2. Genes Dev. 2011, 25:2610-2618.
222. Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J., Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G., Dianov G.L. Ubiquitin ligase ARF-BP1/Mule modulates base excision repair. EMBO J. 2009, 28:3207-3215.
223. Markkanen E., van Loon B., Ferrari E., Parsons J.L., Dianov G.L., Hubscher U. Regulation of oxidative DNA damage repair by DNA polymerase lambda and MutYH by cross-talk of phosphorylation and ubiquitination. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:437-442.
224. Leboucher G.P., Tsai Y.C., Yang M., Shaw K.C., Zhou M., Veenstra T.D., Glickman M.H., Weissman A.M. Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis. Mol. Cell 2012, 47:547-557.
225. Chen D., Brooks C.L., Gu W. ARF-BP1 as a potential therapeutic target. Br. J. Cancer 2006, 94:1555-1558.
226. Confalonieri S., Quarto M., Goisis G., Nuciforo P., Donzelli M., Jodice G., Pelosi G., Viale G., Pece S., Di Fiore P.P. Alterations of ubiquitin ligases in human cancer and their association with the natural history of the tumor. Oncogene 2009, 28:2959-2968.
227. Khoronenkova S.V., Dianov G.L. The emerging role of Mule and ARF in the regulation of base excision repair. FEBS Lett. 2011, 585:2831-2835.
228. Zhao X., D'Arca D., Lim W.K., Brahmachary M., Carro M.S., Ludwig T., Cardo C.C., Guillemot F., Aldape K., Califano A., Iavarone A., Lasorella A. The N-Myc-DLL3 cascade is suppressed by the ubiquitin ligase Huwe1 to inhibit proliferation and promote neurogenesis in the developing brain. Dev. Cell 2009, 17:210-221.
229. Brooks C.L., Gu W. p53 regulation by ubiquitin. FEBS Lett. 2011, 585:2803-2809.
230. Hao Z., Duncan G.S., Su Y.W., Li W.Y., Silvester J., Hong C., You H., Brenner D., Gorrini C., Haight J., Wakeham A., You-Ten A., McCracken S., Elia A., Li Q., Detmar J., Jurisicova A., Hobeika E., Reth M., Sheng Y., Lang P.A., Ohashi P.S., Zhong Q., Wang X., Mak T.W. The E3 ubiquitin ligase Mule acts through the ATM-p53 axis to maintain B lymphocyte homeostasis. J. Exp. Med. 2012, 209:173-186.
231. Kon N., Zhong J., Qiang L., Accili D., Gu W. Inactivation of arf-bp1 induces p53 activation and diabetic phenotypes in mice. J. Biol. Chem. 2012, 287:5102-5111.
232. Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R., Sutherland R.L., Watts C.K. Identification of a human HECT family protein with homology to the Drosophila tumor suppressor gene hyperplastic discs. Oncogene 1998, 17:3479-3491.
233. Deo R.C., Sonenberg N., Burley S.K. X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:4414-4419.
234. Kozlov G., De Crescenzo G., Lim N.S., Siddiqui N., Fantus D., Kahvejian A., Trempe J.F., Elias D., Ekiel I., Sonenberg N., O'Connor-McCourt M., Gehring K. Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase. EMBO J. 2004, 23:272-281.
235. Clancy J.L., Henderson M.J., Russell A.J., Anderson D.W., Bova R.J., Campbell I.G., Choong D.Y., Macdonald G.A., Mann G.J., Nolan T., Brady G., Olopade O.I., Woollatt E., Davies M.J., Segara D., Hacker N.F., Henshall S.M., Sutherland R.L., Watts C.K. EDD, the human orthologue of the hyperplastic discs tumour suppressor gene, is amplified and overexpressed in cancer. Oncogene 2003, 22:5070-5081.
236. Fuja T.J., Lin F., Osann K.E., Bryant P.J. Somatic mutations and altered expression of the candidate tumor suppressors CSNK1 epsilon, DLG1, and EDD/hHYD in mammary ductal carcinoma. Cancer Res. 2004, 64:942-951.
237. Honda Y., Tojo M., Matsuzaki K., Anan T., Matsumoto M., Ando M., Saya H., Nakao M. Cooperation of HECT-domain ubiquitin ligase hHYD and DNA topoisomerase II-binding protein for DNA damage response. J. Biol. Chem. 2002, 277:3599-3605.
238. Yoshida M., Yoshida K., Kozlov G., Lim N.S., De Crescenzo G., Pang Z., Berlanga J.J., Kahvejian A., Gehring K., Wing S.S., Sonenberg N. Poly(A) binding protein (PABP) homeostasis is mediated by the stability of its inhibitor, Paip2. EMBO J. 2006, 25:1934-1944.
239. Hay-Koren A., Caspi M., Zilberberg A., Rosin-Arbesfeld R. The EDD E3 ubiquitin ligase ubiquitinates and up-regulates beta-catenin. Mol. Biol. Cell 2010, 22:399-411.
240. Maddika S., Chen J. Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase. Nat. Cell Biol. 2009, 11:409-419.
241. Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K., Price D.H., Coulombe B. Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B. J. Biol. Chem. 2011, 286:5012-5022.
242. Jiang W., Wang S., Xiao M., Lin Y., Zhou L., Lei Q., Xiong Y., Guan K.L., Zhao S. Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol. Cell 2011, 43:33-44.
243. Gudjonsson T., Altmeyer M., Savic V., Toledo L., Dinant C., Grofte M., Bartkova J., Poulsen M., Oka Y., Bekker-Jensen S., Mailand N., Neumann B., Heriche J.K., Shearer R., Saunders D., Bartek J., Lukas J., Lukas C. TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes. Cell 2012, 150:697-709.
244. Ohshima R., Ohta T., Wu W., Koike A., Iwatani T., Henderson M., Watts C.K., Otsubo T. Putative tumor suppressor EDD interacts with and up-regulates APC. Genes Cells 2007, 12:1339-1345.
245. Henderson M.J., Munoz M.A., Saunders D.N., Clancy J.L., Russell A.J., Williams B., Pappin D., Khanna K.K., Jackson S.P., Sutherland R.L., Watts C.K. EDD mediates DNA damage-induced activation of CHK2. J. Biol. Chem. 2006, 281:39990-40000.
246. Henderson M.J., Russell A.J., Hird S., Munoz M., Clancy J.L., Lehrbach G.M., Calanni S.T., Jans D.A., Sutherland R.L., Watts C.K. EDD, the human hyperplastic discs protein, has a role in progesterone receptor coactivation and potential involvement in DNA damage response. J. Biol. Chem. 2002, 277:26468-26478.
247. Tomaic V., Pim D., Thomas M., Massimi P., Myers M.P., Banks L. Regulation of the human papillomavirus type 18 E6/E6AP ubiquitin ligase complex by the HECT domain-containing protein EDD. J. Virol. 2011, 85:3120-3127.
248. Su H., Meng S., Lu Y., Trombly M.I., Chen J., Lin C., Turk A., Wang X. Mammalian hyperplastic discs homolog EDD regulates miRNA-mediated gene silencing. Mol. Cell 2011, 43:97-109.
249. Chen D., Shan J., Zhu W.G., Qin J., Gu W. Transcription-independent ARF regulation in oncogenic stress-mediated p53 responses. Nature 2010, 464:624-627.
250. Chen D., Yoon J.B., Gu W. Reactivating the ARF-p53 axis in AML cells by targeting ULF. Cell Cycle 2010, 9:2946-2951.
251. Chio M., Sasaki D., Ghazarian J., Moreno S., Done T., Ueda S., Inoue Y.L., Chang N.J., Chen T.W. Mak, TRADD contributes to tumour suppression by regulating ULF-dependent p19Arf ubiquitylation. Nat. Cell Biol. 2012, 14:625-633.
252. Anglesio M.S., Evdokimova V., Melnyk N., Zhang L., Fernandez C.V., Grundy P.E., Leach S., Marra M.A., Brooks-Wilson A.R., Penninger J., Sorensen P.H. Differential expression of a novel ankyrin containing E3 ubiquitin-protein ligase, Hace1, in sporadic Wilms' tumor versus normal kidney. Hum. Mol. Genet. 2004, 13:2061-2074.
253. Zhang L., Anglesio M.S., O'Sullivan M., Zhang F., Yang G., Sarao R., Mai P.N., Cronin S., Hara H., Melnyk N., Li L., Wada T., Liu P.P., Farrar J., Arceci R.J., Sorensen P.H., Penninger J.M. The E3 ligase HACE1 is a critical chromosome 6q21 tumor suppressor involved in multiple cancers. Nat. Med. 2007, 13:1060-1069.
254. Slade I., Stephens P., Douglas J., Barker K., Stebbings L., Abbaszadeh F., Pritchard-Jones K., Cole R., Pizer B., Stiller C., Vujanic G., Scott R.H., Stratton M.R., Rahman N. Constitutional translocation breakpoint mapping by genome-wide paired-end sequencing identifies HACE1 as a putative Wilms tumour susceptibility gene. J. Med. Genet. 2011, 47:342-347.
255. Diskin S.J., Capasso M., Schnepp R.W., Cole K.A., Attiyeh E.F., Hou C., Diamond M., Carpenter E.L., Winter C., Lee H., Jagannathan J., Latorre V., Iolascon A., Hakonarson H., Devoto M., Maris J.M. Common variation at 6q16 within HACE1 and LIN28B influences susceptibility to neuroblastoma. Nat. Genet. 2012, 44:1126-1130.
256. Torrino S., Visvikis O., Doye A., Boyer L., Stefani C., Munro P., Bertoglio J., Gacon G., Mettouchi A., Lemichez E. The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active Rac1. Dev. Cell 2011, 21:959-965.
257. Castillo-Lluva S., Tan C.T., Daugaard M., Sorensen P.H., Malliri A. The tumour suppressor HACE1 controls cell migration by regulating Rac1 degradation. Oncogene 2013, 32:1735-1742.
258. Tang D., Xiang Y., De Renzis S., Rink J., Zheng G., Zerial M., Wang Y. The ubiquitin ligase HACE1 regulates Golgi membrane dynamics during the cell cycle. Nat. Commun. 2011, 2:501.