The role of the transmembrane RING finger proteins in cellular and organelle function

Membranes

Volumn 1, Issue 4, 2011, Pages 354-393

  Nakamura, Nobuhiro ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Endocytosis; ERAD; Immune regulation; Membrane trafficking; Mitochondrial dynamics; Proteasome; Quality control; RNF; Ubiquitin; Ubiquitin ligase

Indexed keywords

ACTIVATION ANALYSIS; CELL MEMBRANES; CYTOLOGY; MAMMALS; MITOCHONDRIA; MOLECULAR BIOLOGY; QUALITY CONTROL;

ENDOCYTOSIS; ERAD; IMMUNE REGULATION; MEMBRANE TRAFFICKING; PROTEASOMES; UBIQUITIN; UBIQUITIN LIGASES;

PROTEINS;

EID: 84055199966     PISSN: None     EISSN: 20770375     Source Type: Journal    
DOI: 10.3390/membranes1040354     Document Type: Review

References (257)

1. Glickman, M.H.; Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol. Rev. 2002, 82, 373-428.
2. Koegl, M.; Hoppe, T.; Schlenker, S.; Ulrich, H.D.; Mayer, T.U.; Jentsch, S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999, 96, 635-644.
3. Ikeda, F.; Dikic, I. Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep. 2008, 9, 536-542.
4. Chau, V.; Tobias, J.W.; Bachmair, A.; Marriott, D.; Ecker, D.J.; Gonda, D.K.; Varshavsky, A. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 1989, 243, 1576-1583.
5. Thrower, J.S.; Hoffman, L.; Rechsteiner, M.; Pickart, C.M. Recognition of the polyubiquitin proteolytic signal. EMBO J. 2000, 19, 94-102.
6. Mukhopadhyay, D.; Riezman, H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 2007, 315, 201-205.
7. Bhoj, V.G.; Chen, Z.J. Ubiquitylation in innate and adaptive immunity. Nature 2009, 458, 430-437.
8. Spence, J.; Sadis, S.; Haas, A.L.; Finley, D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell Biol. 1995, 15, 1265-1273.
9. Hicke, L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2001, 2, 195-201.
10. Reyes-Turcu, F.E.; Ventii, K.H.; Wilkinson, K.D. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem. 2009, 78, 363-397.
11. Welchman, R.L.; Gordon, C.; Mayer, R.J. Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat. Rev. Mol. Cell Biol. 2005, 6, 599-609.
12. Ardley, H.C.; Robinson, P.A. E3 ubiquitin ligases. Essays Biochem. 2005, 41, 15-30.
13. Rotin, D.; Kumar, S. Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2009, 10, 398-409.
14. Borden, K.L.; Boddy, M.N.; Lally, J.; O'Reilly, N.J.; Martin, S.; Howe, K.; Solomon, E.; Freemont, P.S. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. EMBO J. 1995, 14, 1532-1541.
15. Barlow, P.N.; Luisi, B.; Milner, A.; Elliott, M.; Everett, R. Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger. J. Mol. Biol. 1994, 237, 201-211.
16. Dodd, R.B.; Allen, M.D.; Brown, S.E.; Sanderson, C.M.; Duncan, L.M.; Lehner, P.J.; Bycroft, M.; Read, R.J. Solution structure of the Kaposi's sarcoma-associated herpesvirus K3 N-terminal domain reveals a novel E2-binding C4HC3-type RING domain. J. Biol. Chem. 2004, 279, 53840-53847.
17. Deshaies, R.J.; Joazeiro, C.A. RING domain E3 ubiquitin ligases. Annu. Rev. Biochem. 2009, 78, 399-434.
18. Ohi, M.D.; Vander Kooi, C.W.; Rosenberg, J.A.; Chazin, W.J.; Gould, K.L. Structural insights into the U-box, a domain associated with multi-ubiquitination. Nat. Struct. Biol. 2003, 10, 250-255.
19. Cao, Z.; Huett, A.; Kuballa, P.; Giallourakis, C.; Xavier, R.J. DLG1 is an anchor for the E3 ligase MARCH2 at sites of cell-cell contact. Cell Signal 2008, 20, 73-82.
20. Li, W.; Bengtson, M.H.; Ulbrich, A.; Matsuda, A.; Reddy, V.A.; Orth, A.; Chanda, S.K.; Batalov, S.; Joazeiro, C.A. Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling. PLoS One 2008, 3, e1487.
21. Neutzner, A.; Neutzner, M.; Benischke, A.S.; Ryu, S.W.; Frank, S.; Youle, R.J.; Karbowski, M. A systematic search for endoplasmic reticulum (ER) membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis. J. Biol. Chem. 2011, 286, 8633-8643.
22. Thompson, J.D.; Higgins, D.G.; Gibson, T.J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22, 4673-4680.
23. Tamura, K.; Dudley, J.; Nei, M.; Kumar, S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 2007, 24, 1596-1599.
24. Meroni, G.; Diez-Roux, G. TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases. Bioessays 2005, 27, 1147-1157.
25. Massiah, M.A.; Matts, J.A.; Short, K.M.; Simmons, B.N.; Singireddy, S.; Yi, Z.; Cox, T.C. Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: Insights into an evolutionarily conserved RING fold. J. Mol. Biol. 2007, 369, 1-10.
26. Reymond, A.; Meroni, G.; Fantozzi, A.; Merla, G.; Cairo, S.; Luzi, L.; Riganelli, D.; Zanaria, E.; Messali, S.; Cainarca S.; et al. The tripartite motif family identifies cell compartments. EMBO J. 2001, 20, 2140-2151.
27. Sardiello, M.; Cairo, S.; Fontanella, B.; Ballabio, A.; Meroni, G. Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary properties. BMC Evol. Biol. 2008, 8, 225.
28. Ensembl Genome Browser. Cembridge, UK, 2011. Available online: http://www.ensembl.org (accessed on 15 October 2011).
29. National Center for Biotechnology Information. Bethesda, MD, USA, 2011. Available online: http://www.ncbi.nlm.nih.gov (accessed on 15 October 2011).
30. Jin, X.; Cheng, H.; Chen, J.; Zhu, D. RNF13: An emerging RING finger ubiquitin ligase important in cell proliferation. FEBS J. 2011, 278, 78-84.
31. Whiting, C.C.; Su, L.L.; Lin, J.T.; Fathman, C.G. GRAIL: A unique mediator of CD4 T-lymphocyte unresponsiveness. FEBS J. 2011, 278, 47-58.
32. Mahon, P.; Bateman, A. The PA domain: A protease-associated domain. Protein Sci. 2000, 9, 1930-1934.
33. Su, L.L.; Iwai, H.; Lin, J.T.; Fathman, C.G. The transmembrane E3 ligase GRAIL ubiquitinates and degrades CD83 on CD4 T cells. J. Immunol. 2009, 183, 438-444.
34. Lineberry, N.B.; Su, L.L.; Lin, J.T.; Coffey, G.P.; Seroogy, C.M.; Fathman, C.G. Cutting edge: The transmembrane E3 ligase GRAIL ubiquitinates the costimulatory molecule CD40 ligand during the induction of T cell anergy. J. Immunol. 2008, 181, 1622-1626.
35. Bocock, J.P.; Carmicle, S.; Sircar, M.; Erickson, A.H. Trafficking and proteolytic processing of RNF13, a model PA-TM-RING family endosomal membrane ubiquitin ligase. FEBS J. 2011, 278, 69-77.
36. Nathan, J.A.; Lehner, P.J. The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases. Exp. Cell Res. 2009, 315, 1593-1600.
37. Iyengar, P.V.; Hirota, T.; Hirose, S.; Nakamura, N. Membrane-associated RING-CH 10 (MARCH10 protein) is a microtubule-associated E3 ubiquitin ligase of the spermatid flagella. J. Biol. Chem. 2011, 286, 39082-39090.
38. Nathan, J.A.; Sengupta, S.; Wood, S.A.; Admon, A.; Markson, G.; Sanderson, C.; Lehner, P.J. The ubiquitin E3 ligase MARCH7 is differentially regulated by the deubiquitylating enzymes USP7 and USP9X. Traffic 2008, 9, 1130-1145.
39. Bezprozvanny, I.; Maximov, A. Classification of PDZ domains. FEBS Lett. 2001, 509, 457-462.
40. Kay, B.K.; Williamson, M.P.; Sudol, M. The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 2000, 14, 231-241.
41. Eisenhaber, B.; Chumak, N.; Eisenhaber, F.; Hauser, M.T. The ring between ring fingers (RBR) protein family. Genome Biol. 2007, 8, 209.
42. Capili, A.D.; Edghill, E.L.; Wu, K.; Borden, K.L. Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING. J. Mol. Biol. 2004, 340, 1117-1129.
43. Stevens, T.J.; Arkin, I.T. Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins 2000, 39, 417-420.
44. Lander, E.S.; Linton, L.M.; Birren, B.; Nusbaum, C.; Zody, M.C.; Baldwin, J.; Devon, K.; Dewar, K.; Doyle, M.; FitzHugh W.; et al. Initial sequencing and analysis of the human genome. Nature 2001, 409, 860-921.
45. Diehn, M.; Bhattacharya, R.; Botstein, D.; Brown, P.O. Genome-scale identification of membrane-associated human mRNAs. PLoS Genet. 2006, 2, e11.
46. Rapoport, T.A. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 2007, 450, 663-669.
47. Sitia, R.; Braakman, I. Quality control in the endoplasmic reticulum protein factory. Nature 2003, 426, 891-894.
48. Malhotra, J.D.; Kaufman, R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 2007, 18, 716-731.
49. Vembar, S.S.; Brodsky, J.L. One step at a time: Endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 2008, 9, 944-957.
50. Wojcikiewicz, R.J. Regulated ubiquitination of proteins in GPCR-initiated signaling pathways. Trends Pharmacol. Sci. 2004, 25, 35-41.
51. Espenshade, P.J.; Hughes, A.L. Regulation of sterol synthesis in eukaryotes. Annu. Rev. Genet. 2007, 41, 401-427.
52. Shamu, C.E.; Flierman, D.; Ploegh, H.L.; Rapoport, T.A.; Chau, V. Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol. Biol. Cell 2001, 12, 2546-2555.
53. De Virgilio, M.; Weninger, H.; Ivessa, N.E. Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J. Biol. Chem. 1998, 273, 9734-9743.
54. Plemper, R.K.; Bohmler, S.; Bordallo, J.; Sommer, T.; Wolf, D.H. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 1997, 388, 891-895.
55. Meusser, B.; Hirsch, C.; Jarosch, E.; Sommer, T. ERAD: The long road to destruction. Nat. Cell Biol. 2005, 7, 766-772.
56. Wiertz, E.J.; Tortorella, D.; Bogyo, M.; Yu, J.; Mothes, W.; Jones, T.R.; Rapoport, T.A.; Ploegh, H.L. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996, 384, 432-438.
57. Ye, Y.; Meyer, H.H.; Rapoport, T.A. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 2001, 414, 652-656.
58. Jarosch, E.; Taxis, C.; Volkwein, C.; Bordallo, J.; Finley, D.; Wolf, D.H.; Sommer, T. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat. Cell Biol. 2002, 4, 134-139.
59. Braun, S.; Matuschewski, K.; Rape, M.; Thoms, S.; Jentsch, S. Role of the ubiquitin-selective CDC48(UFD1/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 2002, 21, 615-621.
60. Bays, N.W.; Wilhovsky, S.K.; Goradia, A.; Hodgkiss-Harlow, K.; Hampton, R.Y. HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol. Biol. Cell 2001, 12, 4114-4128.
61. Lilley, B.N.; Ploegh, H.L. Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. USA 2005, 102, 14296-14301.
62. Ye, Y.; Shibata, Y.; Kikkert, M.; van Voorden, S.; Wiertz, E.; Rapoport, T.A. Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. USA 2005, 102, 14132-14138.
63. Vashist, S.; Ng, D.T. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J. Cell Biol. 2004, 165, 41-52.
64. Gauss, R.; Jarosch, E.; Sommer, T.; Hirsch, C. A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nat. Cell Biol. 2006, 8, 849-854.
65. Denic, V.; Quan, E.M.; Weissman, J.S. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 2006, 126, 349-359.
66. Carvalho, P.; Goder, V.; Rapoport, T.A. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 2006, 126, 361-373.
67. Biederer, T.; Volkwein, C.; Sommer, T. Role of Cue1p in ubiquitination and degradation at the ER surface. Science 1997, 278, 1806-1809.
68. Deak, P.M.; Wolf, D.H. Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J. Biol. Chem. 2001, 276, 10663-10669.
69. Bays, N.W.; Gardner, R.G.; Seelig, L.P.; Joazeiro, C.A.; Hampton, R.Y. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat. Cell Biol. 2001, 3, 24-29.
70. Swanson, R.; Locher, M.; Hochstrasser, M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev. 2001, 15, 2660-2674.
71. Mehnert, M.; Sommer, T.; Jarosch, E. ERAD ubiquitin ligases: Multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum. Bioessays 2010, 32, 905-913.
72. Feldman, M.; van der Goot, F.G. Novel ubiquitin-dependent quality control in the endoplasmic reticulum. Trends Cell Biol. 2009, 19, 357-363.
73. Hirsch, C.; Gauss, R.; Horn, S.C.; Neuber, O.; Sommer, T. The ubiquitylation machinery of the endoplasmic reticulum. Nature 2009, 458, 453-460.
74. Nadav, E.; Shmueli, A.; Barr, H.; Gonen, H.; Ciechanover, A.; Reiss, Y. A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1. Biochem. Biophys. Res. Commun. 2003, 303, 91-97.
75. Kikkert, M.; Doolman, R.; Dai, M.; Avner, R.; Hassink, G.; van Voorden, S.; Thanedar, S.; Roitelman, J.; Chau, V.; Wiertz, E. Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J. Biol. Chem. 2004, 279, 3525-3534.
76. Christianson, J.C.; Shaler, T.A.; Tyler, R.E.; Kopito, R.R. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 2008, 10, 272-282.
77. Bernasconi, R.; Pertel, T.; Luban, J.; Molinari, M. A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: Inhibiting secretion of misfolded protein conformers and enhancing their disposal. J. Biol. Chem. 2008, 283, 16446-16454.
78. Ye, Y.; Shibata, Y.; Yun, C.; Ron, D.; Rapoport, T.A. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 2004, 429, 841-847.
79. Lilley, B.N.; Ploegh, H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 2004, 429, 834-840.
80. Schulze, A.; Standera, S.; Buerger, E.; Kikkert, M.; van Voorden, S.; Wiertz, E.; Koning, F.; Kloetzel, P.M.; Seeger, M. The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. J. Mol. Biol. 2005, 354, 1021-1027.
81. Kokame, K.; Agarwala, K.L.; Kato, H.; Miyata, T. Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. J. Biol. Chem. 2000, 275, 32846-32853.
82. Mueller, B.; Lilley, B.N.; Ploegh, H.L. SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER. J. Cell Biol. 2006, 175, 261-270.
83. Hosokawa, N.; Wada, I.; Nagasawa, K.; Moriyama, T.; Okawa, K.; Nagata, K. Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP. J. Biol. Chem. 2008, 283, 20914-20924.
84. Oda, Y.; Okada, T.; Yoshida, H.; Kaufman, R.J.; Nagata, K.; Mori, K. Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J. Cell Biol. 2006, 172, 383-393.
85. Chen, B.; Mariano, J.; Tsai, Y.C.; Chan, A.H.; Cohen, M.; Weissman, A.M. The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site. Proc. Natl. Acad. Sci. USA 2006, 103, 341-346.
86. Fang, S.; Ferrone, M.; Yang, C.; Jensen, J.P.; Tiwari, S.; Weissman, A.M. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 2001, 98, 14422-14427.
87. Younger, J.M.; Chen, L.; Ren, H.Y.; Rosser, M.F.; Turnbull, E.L.; Fan, C.Y.; Patterson, C.; Cyr, D.M. Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 2006, 126, 571-582.
88. Matsuda, N.; Suzuki, T.; Tanaka, K.; Nakano, A. Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase. J. Cell Sci. 2001, 114, 1949-1957.
89. Tsai, Y.C.; Mendoza, A.; Mariano, J.M.; Zhou, M.; Kostova, Z.; Chen, B.; Veenstra, T.; Hewitt, S.M.; Helman, L.J.; Khanna, C.; Weissman, A.M. The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation. Nat. Med. 2007, 13, 1504-1509.
90. Song, B.L.; Sever, N.; DeBose-Boyd, R.A. Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Mol. Cell 2005, 19, 829-840.
91. Liang, J.S.; Kim, T.; Fang, S.; Yamaguchi, J.; Weissman, A.M.; Fisher, E.A.; Ginsberg, H.N. Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells. J. Biol. Chem. 2003, 278, 23984-23988.
92. Morito, D.; Hirao, K.; Oda, Y.; Hosokawa, N.; Tokunaga, F.; Cyr, D.M.; Tanaka, K.; Iwai, K.; Nagata, K. Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508. Mol. Biol. Cell 2008, 19, 1328-1336.
93. Kreft, S.G.; Wang, L.; Hochstrasser, M. Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J. Biol. Chem. 2006, 281, 4646-4653.
94. Hassink, G.; Kikkert, M.; van Voorden, S.; Lee, S.J.; Spaapen, R.; van Laar, T.; Coleman, C.S.; Bartee, E.; Fruh, K.; Chau, V.; et al. TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum. Biochem. J. 2005, 388, 647-655.
95. Zavacki, A.M.; Arrojo, E.D.R.; Freitas, B.C.; Chung, M.; Harney, J.W.; Egri, P.; Wittmann, G.; Fekete, C.; Gereben, B.; Bianco, A.C. The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase. Mol. Cell Biol. 2009, 29, 5339-5347.
96. Wang, L.; Dong, H.; Soroka, C.J.; Wei, N.; Boyer, J.L.; Hochstrasser, M. Degradation of the bile salt export pump at endoplasmic reticulum in progressive familial intrahepatic cholestasis type II. Hepatology 2008, 48, 1558-1569.
97. Yasojima, K.; Tsujimura, A.; Mizuno, T.; Shigeyoshi, Y.; Inazawa, J.; Kikuno, R.; Kuma, K.; Ohkubo, K.; Hosokawa, Y.; Ibata, Y.; et al. Cloning of human and mouse cDNAs encoding novel zinc finger proteins expressed in cerebellum and hippocampus. Biochem. Biophys. Res. Commun. 1997, 231, 481-487.
98. Maruyama, Y.; Yamada, M.; Takahashi, K. Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated degradation pathway. Biochem. Biophys. Res. Commun. 2008, 374, 737-741.
99. Nishioka, G.; Yamada, M.; Kudo, K.; Takahashi, K.; Kiuchi, Y.; Higuchi, T.; Momose, K.; Kamijima, K. Induction of kf-1 after repeated electroconvulsive treatment and chronic antidepressant treatment in rat frontal cortex and hippocampus. J. Neural Transm. 2003, 110, 277-285.
100. Yamada, M.; Yamazaki, S.; Takahashi, K.; Nishioka, G.; Kudo, K.; Ozawa, H.; Yamada, S.; Kiuchi, Y.; Kamijima, K.; Higuchi, T.; et al. Identification of a novel gene with RING-H2 finger motif induced after chronic antidepressant treatment in rat brain. Biochem. Biophys. Res. Commun. 2000, 278, 150-157.
101. Hashimoto-Gotoh, T.; Iwabe, N.; Tsujimura, A.; Nakagawa, M.; Marunaka, Y. KF-1 ubiquitin ligase: Anxiety suppressor model. Cell Biochem. Biophys. 2011, 60, 69-75.
102. Altier, C.; Garcia-Caballero, A.; Simms, B.; You, H.; Chen, L.; Walcher, J.; Tedford, H.W.; Hermosilla, T.; Zamponi, G.W. The Cavbeta subunit prevents RFP2-mediated ubiquitination and proteasomal degradation of L-type channels. Nat. Neurosci. 2011, 14, 173-180.
103. Lerner, M.; Corcoran, M.; Cepeda, D.; Nielsen, M.L.; Zubarev, R.; Ponten, F.; Uhlen, M.; Hober, S.; Grander, D.; Sangfelt, O. The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD. Mol. Biol. Cell 2007, 18, 1670-1682.
104. Goldstein, J.L.; DeBose-Boyd, R.A.; Brown, M.S. Protein sensors for membrane sterols. Cell 2006, 124, 35-46.
105. Gemmill, R.M.; Bemis, L.T.; Lee, J.P.; Sozen, M.A.; Baron, A.; Zeng, C.; Erickson, P.F.; Hooper, J.E.; Drabkin, H.A. The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway. Oncogene 2002, 21, 3507-3516.
106. Gemmill, R.M.; West, J.D.; Boldog, F.; Tanaka, N.; Robinson, L.J.; Smith, D.I.; Li, F.; Drabkin, H.A. The hereditary renal cell carcinoma 3;8 translocation fuses FHIT to a patched-related gene, TRC8. Proc. Natl. Acad. Sci. USA 1998, 95, 9572-9577.
107. Irisawa, M.; Inoue, J.; Ozawa, N.; Mori, K.; Sato, R. The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage. J. Biol. Chem. 2009, 284, 28995-29004.
108. Lee, J.P.; Brauweiler, A.; Rudolph, M.; Hooper, J.E.; Drabkin, H.A.; Gemmill, R.M. The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways. Mol. Cancer Res. 2010, 8, 93-106.
109. Lu, J.P.; Wang, Y.; Sliter, D.A.; Pearce, M.M.; Wojcikiewicz, R.J. title typecontributorRNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. J. Biol. Chem. 2011, 286, 24426-24433.
110. Valdmanis, P.N.; Dupre, N.; Lachance, M.; Stochmanski, S.J.; Belzil, V.V.; Dion, P.A.; Thiffault, I.; Brais, B.; Weston, L.; Saint-Amant, L.; Samuels, M.E.; Rouleau, G.A. A mutation in the RNF170 gene causes autosomal dominant sensory ataxia. Brain 2011, 134, 602-607.
111. Brown, E.M.; MacLeod, R.J. Extracellular calcium sensing and extracellular calcium signaling. Physiol. Rev. 2001, 81, 239-297.
112. Huang, Y.; Niwa, J.; Sobue, G.; Breitwieser, G.E. Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. J. Biol. Chem. 2006, 281, 11610-11617.
113. Niwa, J.; Ishigaki, S.; Hishikawa, N.; Yamamoto, M.; Doyu, M.; Murata, S.; Tanaka, K.; Taniguchi, N.; Sobue, G. Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity. J. Biol. Chem. 2002, 277, 36793-36798.
114. Sone, J.; Niwa, J.; Kawai, K.; Ishigaki, S.; Yamada, S.; Adachi, H.; Katsuno, M.; Tanaka, F.; Doyu, M.; Sobue, G. Dorfin ameliorates phenotypes in a transgenic mouse model of amyotrophic lateral sclerosis. J. Neurosci. Res. 2010, 88, 123-135.
115. Niwa, J.; Yamada, S.; Ishigaki, S.; Sone, J.; Takahashi, M.; Katsuno, M.; Tanaka, F.; Doyu, M.; Sobue, G. Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1. J. Biol. Chem. 2007, 282, 28087-28095.
116. Takeuchi, H.; Niwa, J.; Hishikawa, N.; Ishigaki, S.; Tanaka, F.; Doyu, M.; Sobue, G. Dorfin prevents cell death by reducing mitochondrial localizing mutant superoxide dismutase 1 in a neuronal cell model of familial amyotrophic lateral sclerosis. J. Neurochem. 2004, 89, 64-72.
117. Rong, J.; Chen, L.; Toth, J.I.; Tcherpakov, M.; Petroski, M.D.; Reed, J.C. Bifunctional apoptosis regulator (BAR), an endoplasmic reticulum (ER)-associated E3 ubiquitin ligase, modulates BI-1 protein stability and function in ER Stress. J. Biol. Chem. 2011, 286, 1453-1463.
118. Cox, J.S.; Shamu, C.E.; Walter, P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 1993, 73, 1197-1206.
119. Yoshida, H.; Matsui, T.; Yamamoto, A.; Okada, T.; Mori, K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001, 107, 881-891.
120. Calfon, M.; Zeng, H.; Urano, F.; Till, J.H.; Hubbard, S.R.; Harding, H.P.; Clark, S.G.; Ron, D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 2002, 415, 92-96.
121. Urano, F.; Wang, X.; Bertolotti, A.; Zhang, Y.; Chung, P.; Harding, H.P.; Ron, D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000, 287, 664-666.
122. Peng, Z.; Shi, T.; Ma, D. RNF122: A novel ubiquitin ligase associated with calcium-modulating cyclophilin ligand. BMC Cell Biol. 2010, 11, 41.
123. Ogawa, M.; Mizugishi, K.; Ishiguro, A.; Koyabu, Y.; Imai, Y.; Takahashi, R.; Mikoshiba, K.; Aruga, J. Rines/RNF180, a novel RING finger gene-encoded product, is a membrane-bound ubiquitin ligase. Genes Cells 2008, 13, 397-409.
124. Zhang, Q.; Wang, K.; Zhang, Y.; Meng, J.; Yu, F.; Chen, Y.; Zhu, D. The myostatin-induced E3 ubiquitin ligase RNF13 negatively regulates the proliferation of chicken myoblasts. FEBS J. 2010, 277, 466-476.
125. Bocock, J.P.; Carmicle, S.; Chhotani, S.; Ruffolo, M.R.; Chu, H.; Erickson, A.H. The PA-TM-RING protein RING finger protein 13 is an endosomal integral membrane E3 ubiquitin ligase whose RING finger domain is released to the cytoplasm by proteolysis. FEBS J. 2009, 276, 1860-1877.
126. Zhang, Q.; Meng, Y.; Zhang, L.; Chen, J.; Zhu, D. RNF13: A novel RING-type ubiquitin ligase over-expressed in pancreatic cancer. Cell Res. 2009, 19, 348-357.
127. Bocock, J.P.; Carmicle, S.; Madamba, E.; Erickson, A.H. Nuclear targeting of an endosomal E3 ubiquitin ligase. Traffic 2010, 11, 756-766.
128. Schultz, N.; Hamra, F.K.; Garbers, D.L. A multitude of genes expressed solely in meiotic or postmeiotic spermatogenic cells offers a myriad of contraceptive targets. Proc. Natl. Acad. Sci. USA 2003, 100, 12201-12206.
129. Nian, H.; Zhang, W.; Shi, H.; Zhao, Q.; Xie, Q.; Liao, S.; Zhang, Y.; Zhang, Z.; Wang, C.; Han, C. Mouse RING finger protein Rnf133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase. Cell Res. 2008, 18, 800-802.
130. Rivkin, E.; Kierszenbaum, A.L.; Gil, M.; Tres, L.L. Rnf19a, a ubiquitin protein ligase, and Psmc3, a component of the 26S proteasome, tether to the acrosome membranes and the head-tail coupling apparatus during rat spermatid development. Dev. Dyn. 2009, 238, 1851-1861.
131. French, L.E.; Tschopp, J. Protein-based therapeutic approaches targeting death receptors. Cell Death Differ. 2003, 10, 117-123.
132. Garrido, C.; Galluzzi, L.; Brunet, M.; Puig, P.E.; Didelot, C.; Kroemer, G. Mechanisms of cytochrome c release from mitochondria. Cell Death Differ. 2006, 13, 1423-1433.
133. Gross, A.; McDonnell, J.M.; Korsmeyer, S.J. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 1999, 13, 1899-1911.
134. Zhang, H.; Xu, Q.; Krajewski, S.; Krajewska, M.; Xie, Z.; Fuess, S.; Kitada, S.; Pawlowski, K.; Godzik, A.; Reed, J.C. BAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins. Proc. Natl. Acad. Sci. USA 2000, 97, 2597-2602.
135. Roth, W.; Kermer, P.; Krajewska, M.; Welsh, K.; Davis, S.; Krajewski, S.; Reed, J.C. Bifunctional apoptosis inhibitor (BAR) protects neurons from diverse cell death pathways. Cell Death Differ. 2003, 10, 1178-1187.
136. Oren, M. Decision making by p53: Life, death and cancer. Cell Death Differ. 2003, 10, 431-442.
137. Ng, C.C.; Arakawa, H.; Fukuda, S.; Kondoh, H.; Nakamura, Y. p53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1. Oncogene 2003, 22, 4449-4458.
138. Huang, J.; Xu, L.G.; Liu, T.; Zhai, Z.; Shu, H.B. The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis. FEBS Lett. 2006, 580, 940-947.
139. Sayan, B.S.; Yang, A.L.; Conforti, F.; Tucci, P.; Piro, M.C.; Browne, G.J.; Agostini, M.; Bernardini, S.; Knight, R.A.; Mak, T.W.; et al. Differential control of TAp73 and DeltaNp73 protein stability by the ring finger ubiquitin ligase PIR2. Proc. Natl. Acad. Sci. USA 2010, 107, 12877-12882.
140. Ishimoto, O.; Kawahara, C.; Enjo, K.; Obinata, M.; Nukiwa, T.; Ikawa, S. Possible oncogenic potential of DeltaNp73: A newly identified isoform of human p73. Cancer Res. 2002, 62, 636-641.
141. Jost, C.A.; Marin, M.C.; Kaelin, W.G., Jr. p73 is a simian [correction of human] p53-related protein that can induce apoptosis. Nature 1997, 389, 191-194.
142. Maisse, C.; Munarriz, E.; Barcaroli, D.; Melino, G.; De Laurenzi, V. DNA damage induces the rapid and selective degradation of the DeltaNp73 isoform, allowing apoptosis to occur. Cell Death Differ. 2004, 11, 685-687.
143. Benard, G.; Neutzner, A.; Peng, G.; Wang, C.; Livak, F.; Youle, R.J.; Karbowski, M. IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation. EMBO J. 2010, 29, 1458-1471.
144. Liu, Q.Y.; Lei, J.X.; Sikorska, M.; Liu, R. A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the brains of Alzheimer's patients and targets ATP6V0C for degradation. Mol. Neurodegener. 2008, 3, 4.
145. Joo, H.M.; Kim, J.Y.; Jeong, J.B.; Seong, K.M.; Nam, S.Y.; Yang, K.H.; Kim, C.S.; Kim, H.S.; Jeong, M.; An, S.; Ret finger protein 2 enhances ionizing radiation-induced apoptosis via degradation of AKT and MDM2. Eur J. Cell Biol. 2011, 90, 420-431.
146. Guicciardi, M.E.; Leist, M.; Gores, G.J. Lysosomes in cell death. Oncogene 2004, 23, 2881-2890.
147. Zhang, S.; Wu, W.; Wu, Y.; Zheng, J.; Suo, T.; Tang, H.; Tang, J. RNF152, a novel lysosome localized E3 ligase with pro-apoptotic activities. Protein Cell 2010, 1, 656-663.
148. Wilson, C.; Ragnini-Wilson, A. Conserved molecular mechanisms underlying homeostasis of the Golgi complex. Int. J. Cell Biol. 2010, 2010, 758230.
149. Sciaky, N.; Presley, J.; Smith, C.; Zaal, K.J.; Cole, N.; Moreira, J.E.; Terasaki, M.; Siggia, E.; Lippincott-Schwartz, J. Golgi tubule traffic and the effects of brefeldin A visualized in living cells. J. Cell Biol. 1997, 139, 1137-1155.
150. Ramirez, I.B.; Lowe, M. Golgins and GRASPs: Holding the Golgi together. Semin. Cell Dev. Biol. 2009, 20, 770-779.
151. Barr, F.A.; Nakamura, N.; Warren, G. Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae. EMBO J. 1998, 17, 3258-3268.
152. Barr, F.A.; Puype, M.; Vandekerckhove, J.; Warren, G. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 1997, 91, 253-262.
153. Nakamura, N.; Lowe, M.; Levine, T.P.; Rabouille, C.; Warren, G. The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 1997, 89, 445-455.
154. Lesa, G.M.; Seemann, J.; Shorter, J.; Vandekerckhove, J.; Warren, G. The amino-terminal domain of the golgi protein giantin interacts directly with the vesicle-tethering protein p115. J. Biol. Chem. 2000, 275, 2831-2836.
155. Diao, A.; Frost, L.; Morohashi, Y.; Lowe, M. Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin 5 in a p115-regulated manner. J. Biol. Chem. 2008, 283, 6957-6967.
156. Chiu, C.F.; Ghanekar, Y.; Frost, L.; Diao, A.; Morrison, D.; McKenzie, E.; Lowe, M. ZFPL1, a novel ring finger protein required for cis-Golgi integrity and efficient ER-to-Golgi transport. EMBO J. 2008, 27, 934-947.
157. Dupre, S.; Urban-Grimal, D.; Haguenauer-Tsapis, R. Ubiquitin and endocytic internalization in yeast and animal cells. Biochim. Biophys. Acta 2004, 1695, 89-111.
158. Piper, R.C.; Luzio, J.P. Ubiquitin-dependent sorting of integral membrane proteins for degradation in lysosomes. Curr. Opin. Cell Biol. 2007, 19, 459-465.
159. Ren, X.; Hurley, J.H. VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo. EMBO J. 2010, 29, 1045-1054.
160. Katzmann, D.J.; Babst, M.; Emr, S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 2001, 106, 145-155.
161. Raiborg, C.; Stenmark, H. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 2009, 458, 445-452.
162. Ishido, S.; Matsuki, Y.; Goto, E.; Kajikawa, M.; Ohmura-Hoshino, M. MARCH-I: A new regulator of dendritic cell function. Mol. Cells 2010, 29, 229-232.
163. Goto, E.; Ishido, S.; Sato, Y.; Ohgimoto, S.; Ohgimoto, K.; Nagano-Fujii, M.; Hotta, H. c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity. J. Biol. Chem. 2003, 278, 14657-14668.
164. Bartee, E.; Mansouri, M.; Hovey Nerenberg, B.T.; Gouveia, K.; Fruh, K. Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J. Virol. 2004, 78, 1109-1120.
165. Ohmura-Hoshino, M.; Matsuki, Y.; Aoki, M.; Goto, E.; Mito, M.; Uematsu, M.; Kakiuchi, T.; Hotta, H.; Ishido, S. Inhibition of MHC class II expression and immune responses by c-MIR. J. Immunol. 2006, 177, 341-354.
166. Goto, E.; Mito-Yoshida, M.; Uematsu, M.; Aoki, M.; Matsuki, Y.; Ohmura-Hoshino, M.; Hotta, H.; Miyagishi, M.; Ishido, S. An excellent monitoring system for surface ubiquitination-induced internalization in mammals. PLoS One 2008, 3, e1490.
167. Matsuki, Y.; Ohmura-Hoshino, M.; Goto, E.; Aoki, M.; Mito-Yoshida, M.; Uematsu, M.; Hasegawa, T.; Koseki, H.; Ohara, O.; Nakayama, M.; et al. Novel regulation of MHC class II function in B cells. EMBO J. 2007, 26, 846-854.
168. Baravalle, G.; Park, H.; McSweeney, M.; Ohmura-Hoshino, M.; Matsuki, Y.; Ishido, S.; Shin, J.S. Ubiquitination of CD86 is a key mechanism in regulating antigen presentation by dendritic cells. J. Immunol. 2011, 187, 2966-2973.
169. Corcoran, K.; Jabbour, M.; Bhagwandin, C.; Deymier, M.J.; Theisen, D.L.; Lybarger, L. Ubiquitin-mediated regulation of CD86 expression by membrane-associated RING-CH1 (MARCH1). J. Biol. Chem. 2011, 286, 37168-37180.
170. Ohmura-Hoshino, M.; Matsuki, Y.; Mito-Yoshida, M.; Goto, E.; Aoki-Kawasumi, M.; Nakayama, M.; Ohara, O.; Ishido, S. Cutting edge: Requirement of MARCH-I-mediated MHC II ubiquitination for the maintenance of conventional dendritic cells. J. Immunol. 2009, 183, 6893-6897.
171. Walseng, E.; Furuta, K.; Bosch, B.; Weih, K.A.; Matsuki, Y.; Bakke, O.; Ishido, S.; Roche, P.A. Ubiquitination regulates MHC class II-peptide complex retention and degradation in dendritic cells. Proc. Natl. Acad. Sci. USA 2010, 107, 20465-20470.
172. Walseng, E.; Furuta, K.; Goldszmid, R.S.; Weih, K.A.; Sher, A.; Roche, P.A. Dendritic cell activation prevents MHC class II ubiquitination and promotes MHC class II survival regardless of the activation stimulus. J. Biol. Chem. 2010, 285, 41749-41754.
173. Van Niel, G.; Wubbolts, R.; Ten Broeke, T.; Buschow, S.I.; Ossendorp, F.A.; Melief, C.J.; Raposo, G.; van Balkom, B.W.; Stoorvogel, W. Dendritic cells regulate exposure of MHC class II at their plasma membrane by oligoubiquitination. Immunity 2006, 25, 885-894.
174. Jabbour, M.; Campbell, E.M.; Fares, H.; Lybarger, L. Discrete domains of MARCH1 mediate its localization, functional interactions, and posttranscriptional control of expression. J. Immunol. 2009, 183, 6500-6512.
175. De Gassart, A.; Camosseto, V.; Thibodeau, J.; Ceppi, M.; Catalan, N.; Pierre, P.; Gatti, E. MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation. Proc. Natl. Acad. Sci. USA 2008, 105, 3491-3496.
176. Tze, L.E.; Horikawa, K.; Domaschenz, H.; Howard, D.R.; Roots, C.M.; Rigby, R.J.; Way, D.A.; Ohmura-Hoshino, M.; Ishido, S.; Andoniou, C.E.; et al. CD83 increases MHC II and CD86 on dendritic cells by opposing IL-10-driven MARCH1-mediated ubiquitination and degradation. J. Exp. Med. 2011, 208, 149-165.
177. Pletinckx, K.; Dohler, A.; Pavlovic, V.; Lutz, M.B. Role of dendritic cell maturity/costimulation for generation, homeostasis and suppressive activity of regulatory T cells. Front. Immunol. 2011, 2, 39.
178. Corinti, S.; Albanesi, C.; la Sala, A.; Pastore, S.; Girolomoni, G. Regulatory activity of autocrine IL-10 on dendritic cell functions. J. Immunol. 2001, 166, 4312-4318.
179. Thibodeau, J.; Bourgeois-Daigneault, M.C.; Huppe, G.; Tremblay, J.; Aumont, A.; Houde, M.; Bartee, E.; Brunet, A.; Gauvreau, M.E.; de Gassart, A.; et al. Interleukin-10-induced MARCH1 mediates intracellular sequestration of MHC class II in monocytes. Eur. J. Immunol. 2008, 38, 1225-1230.
180. Hor, S.; Ziv, T.; Admon, A.; Lehner, P.J. Stable isotope labeling by amino acids in cell culture and differential plasma membrane proteome quantitation identify new substrates for the MARCH9 transmembrane E3 ligase. Mol. Cell Proteomics 2009, 8, 1959-1971.
181. Hoer, S.; Smith, L.; Lehner, P.J. MARCH-IX mediates ubiquitination and downregulation of ICAM-1. FEBS Lett. 2007, 581, 45-51.
182. Nice, T.J.; Deng, W.; Coscoy, L.; Raulet, D.H. Stress-regulated targeting of the NKG2D ligand Mult1 by a membrane-associated RING-CH family E3 ligase. J. Immunol. 2010, 185, 5369-5376.
183. Barriere, H.; Nemes, C.; Du, K.; Lukacs, G.L. Plasticity of polyubiquitin recognition as lysosomal targeting signals by the endosomal sorting machinery. Mol. Biol. Cell 2007, 18, 3952-3965.
184. Eyster, C.A.; Cole, N.B.; Petersen, S.; Viswanathan, K.; Fruh, K.; Donaldson, J.G. MARCH ubiquitin ligases alter the itinerary of clathrin-independent cargo from recycling to degradation. Mol. Biol. Cell 2011, 22, 3218-3230.
185. Appleman, L.J.; Boussiotis, V.A. T cell anergy and costimulation. Immunol. Rev. 2003, 192, 161-180.
186. Schwartz, R.H. T cell anergy. Annu. Rev. Immunol. 2003, 21, 305-334.
187. Anandasabapathy, N.; Ford, G.S.; Bloom, D.; Holness, C.; Paragas, V.; Seroogy, C.; Skrenta, H.; Hollenhorst, M.; Fathman, C.G.; Soares, L. GRAIL: An E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells. Immunity 2003, 18, 535-547.
188. Heissmeyer, V.; Macian, F.; Im, S.H.; Varma, R.; Feske, S.; Venuprasad, K.; Gu, H.; Liu, Y.C.; Dustin, M.L.; Rao, A. Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins. Nat. Immunol. 2004, 5, 255-265.
189. Seroogy, C.M.; Soares, L.; Ranheim, E.A.; Su, L.; Holness, C.; Bloom, D.; Fathman, C.G. The gene related to anergy in lymphocytes, an E3 ubiquitin ligase, is necessary for anergy induction in CD4 T cells. J. Immunol. 2004, 173, 79-85.
190. Lineberry, N.; Su, L.; Soares, L.; Fathman, C.G. The single subunit transmembrane E3 ligase gene related to anergy in lymphocytes (GRAIL) captures and then ubiquitinates transmembrane proteins across the cell membrane. J. Biol. Chem. 2008, 283, 28497-28505.
191. Su, L.; Lineberry, N.; Huh, Y.; Soares, L.; Fathman, C.G. A novel E3 ubiquitin ligase substrate screen identifies Rho guanine dissociation inhibitor as a substrate of gene related to anergy in lymphocytes. J. Immunol. 2006, 177, 7559-7566.
192. Kriegel, M.A.; Rathinam, C.; Flavell, R.A. E3 ubiquitin ligase GRAIL controls primary T cell activation and oral tolerance. Proc. Natl. Acad. Sci. USA 2009, 106, 16770-16775.
193. Johannes, L.; Wunder, C. Retrograde transport: Two (or more) roads diverged in an endosomal tree? Traffic 2011, 12, 956-962.
194. Jahn, R.; Scheller, R.H. SNAREs-Engines for membrane fusion. Nat. Rev. Mol. Cell Biol. 2006, 7, 631-643.
195. Ganley, I.G.; Espinosa, E.; Pfeffer, S.R. A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells. J. Cell Biol. 2008, 180, 159-172.
196. Mallard, F.; Tang, B.L.; Galli, T.; Tenza, D.; Saint-Pol, A.; Yue, X.; Antony, C.; Hong, W.; Goud, B.; Johannes, L. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J. Cell Biol. 2002, 156, 653-664.
197. Nakamura, N.; Fukuda, H.; Kato, A.; Hirose, S. MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking. Mol. Biol. Cell 2005, 16, 1696-1710.
198. Fukuda, H.; Nakamura, N.; Hirose, S. MARCH-III Is a novel component of endosomes with properties similar to those of MARCH-II. J. Biochem. 2006, 139, 137-145.
199. Morokuma, Y.; Nakamura, N.; Kato, A.; Notoya, M.; Yamamoto, Y.; Sakai, Y.; Fukuda, H.; Yamashina, S.; Hirata, Y.; Hirose, S. MARCH-XI, a novel transmembrane ubiquitin ligase implicated in ubiquitin-dependent protein sorting in developing spermatids. J. Biol. Chem. 2007, 282, 24806-24815.
200. Meyer, C.; Zizioli, D.; Lausmann, S.; Eskelinen, E.L.; Hamann, J.; Saftig, P.; von Figura, K.; Schu, P. mu1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 2000, 19, 2193-2203.
201. Ramalho-Santos, J.; Schatten, G.; Moreno, R.D. Control of membrane fusion during spermiogenesis and the acrosome reaction. Biol. Reprod. 2002, 67, 1043-1051.
202. Moreno, R.D. Differential expression of lysosomal associated membrane protein (LAMP-1) during mammalian spermiogenesis. Mol. Reprod. Dev. 2003, 66, 202-209.
203. Martinez-Menarguez, J.A.; Geuze, H.J.; Ballesta, J. Evidence for a nonlysosomal origin of the acrosome. J. Histochem. Cytochem. 1996, 44, 313-320.
204. Kang-Decker, N.; Mantchev, G.T.; Juneja, S.C.; McNiven, M.A.; van Deursen, J.M. Lack of acrosome formation in Hrb-deficient mice. Science 2001, 294, 1531-1533.
205. Yao, R.; Ito, C.; Natsume, Y.; Sugitani, Y.; Yamanaka, H.; Kuretake, S.; Yanagida, K.; Sato, A.; Toshimori, K.; Noda, T. Lack of acrosome formation in mice lacking a Golgi protein, GOPC. Proc. Natl. Acad. Sci. USA 2002, 99, 11211-11216.
206. Scott, P.M.; Bilodeau, P.S.; Zhdankina, O.; Winistorfer, S.C.; Hauglund, M.J.; Allaman, M.M.; Kearney, W.R.; Robertson, A.D.; Boman, A.L.; Piper, R.C. GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network. Nat. Cell Biol. 2004, 6, 252-259.
207. Puertollano, R.; Bonifacino, J.S. Interactions of GGA3 with the ubiquitin sorting machinery. Nat. Cell Biol. 2004, 6, 244-251.
208. Berruti, G.; Ripolone, M.; Ceriani, M. USP8, a regulator of endosomal sorting, is involved in mouse acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Biol. Reprod. 2010, 82, 930-939.
209. Haraguchi, C.M.; Mabuchi, T.; Hirata, S.; Shoda, T.; Hoshi, K.; Yokota, S. Ubiquitin signals in the developing acrosome during spermatogenesis of rat testis: An immunoelectron microscopic study. J. Histochem. Cytochem. 2004, 52, 1393-1403.
210. Westermann, B. Mitochondrial fusion and fission in cell life and death. Nat. Rev. Mol. Cell Biol. 2010, 11, 872-884.
211. Hales, K.G.; Fuller, M.T. Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase. Cell 1997, 90, 121-129.
212. Smirnova, E.; Griparic, L.; Shurland, D.L.; van der Bliek, A.M. Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell 2001, 12, 2245-2256.
213. Bleazard, W.; McCaffery, J.M.; King, E.J.; Bale, S.; Mozdy, A.; Tieu, Q.; Nunnari, J.; Shaw, J.M. The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast. Nat. Cell Biol. 1999, 1, 298-304.
214. Otsuga, D.; Keegan, B.R.; Brisch, E.; Thatcher, J.W.; Hermann, G.J.; Bleazard, W.; Shaw, J.M. The dynamin-related GTPase, Dnm1p, controls mitochondrial morphology in yeast. J. Cell Biol. 1998, 143, 333-349.
215. Wong, E.D.; Wagner, J.A.; Gorsich, S.W.; McCaffery, J.M.; Shaw, J.M.; Nunnari, J. The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria. J. Cell Biol. 2000, 151, 341-352.
216. Shepard, K.A.; Yaffe, M.P. The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance. J. Cell Biol. 1999, 144, 711-720.
217. Hermann, G.J.; Thatcher, J.W.; Mills, J.P.; Hales, K.G.; Fuller, M.T.; Nunnari, J.; Shaw, J.M. Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p. J. Cell Biol. 1998, 143, 359-373.
218. Rapaport, D.; Brunner, M.; Neupert, W.; Westermann, B. Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae. J. Biol. Chem. 1998, 273, 20150-20155.
219. Olichon, A.; Baricault, L.; Gas, N.; Guillou, E.; Valette, A.; Belenguer, P.; Lenaers, G. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 2003, 278, 7743-7746.
220. Santel, A.; Fuller, M.T. Control of mitochondrial morphology by a human mitofusin. J. Cell Sci. 2001, 114, 867-874.
221. Chen, H.; Detmer, S.A.; Ewald, A.J.; Griffin, E.E.; Fraser, S.E.; Chan, D.C. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 2003, 160, 189-200.
222. Alexander, C.; Votruba, M.; Pesch, U.E.; Thiselton, D.L.; Mayer, S.; Moore, A.; Rodriguez, M.; Kellner, U.; Leo-Kottler, B.; Auburger, G.; Bhattacharya, S.S.; Wissinger, B. OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat. Genet. 2000, 26, 211-215.
223. Delettre, C.; Lenaers, G.; Griffoin, J.M.; Gigarel, N.; Lorenzo, C.; Belenguer, P.; Pelloquin, L.; Grosgeorge, J.; Turc-Carel, C.; Perret, E.; Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy. Nat. Genet. 2000, 26, 207-210.
224. Zuchner, S.; Mersiyanova, I.V.; Muglia, M.; Bissar-Tadmouri, N.; Rochelle, J.; Dadali, E.L.; Zappia, M.; Nelis, E.; Patitucci, A.; Senderek, J.; Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A. Nat. Genet. 2004, 36, 449-451.
225. Wakabayashi, J.; Zhang, Z.; Wakabayashi, N.; Tamura, Y.; Fukaya, M.; Kensler, T.W.; Iijima, M.; Sesaki, H. The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice. J. Cell Biol. 2009, 186, 805-816.
226. Ishihara, N.; Nomura, M.; Jofuku, A.; Kato, H.; Suzuki, S.O.; Masuda, K.; Otera, H.; Nakanishi, Y.; Nonaka, I.; Goto, Y.; Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice. Nat. Cell Biol. 2009, 11, 958-966.
227. Rinaldi, T.; Ricci, C.; Porro, D.; Bolotin-Fukuhara, M.; Frontali, L. A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology. Mol. Biol. Cell 1998, 9, 2917-2931.
228. Fisk, H.A.; Yaffe, M.P. A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 1999, 145, 1199-1208.
229. Escobar-Henriques, M.; Westermann, B.; Langer, T. Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1. J. Cell Biol. 2006, 173, 645-650.
230. Fritz, S.; Weinbach, N.; Westermann, B. Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. Mol. Biol. Cell 2003, 14, 2303-2313.
231. Cohen, M.M.; Amiott, E.A.; Day, A.R.; Leboucher, G.P.; Pryce, E.N.; Glickman, M.H.; McCaffery, J.M.; Shaw, J.M.; Weissman, A.M. Sequential requirements for the GTPase domain of the mitofusin Fzo1 and the ubiquitin ligase SCFMdm30 in mitochondrial outer membrane fusion. J. Cell Sci. 2011, 124, 1403-1410.
232. Cohen, M.M.; Leboucher, G.P.; Livnat-Levanon, N.; Glickman, M.H.; Weissman, A.M. Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical regulator of mitochondrial fusion. Mol. Biol. Cell 2008, 19, 2457-2464.
233. Nakamura, N.; Kimura, Y.; Tokuda, M.; Honda, S.; Hirose, S. MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep. 2006, 7, 1019-1022.
234. Yonashiro, R.; Ishido, S.; Kyo, S.; Fukuda, T.; Goto, E.; Matsuki, Y.; Ohmura-Hoshino, M.; Sada, K.; Hotta, H.; Yamamura, H.; Inatome, R.; Yanagi, S. A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics. EMBO J. 2006, 25, 3618-3626.
235. Karbowski, M.; Neutzner, A.; Youle, R.J. The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. J. Cell Biol. 2007, 178, 71-84.
236. Park, Y.Y.; Lee, S.; Karbowski, M.; Neutzner, A.; Youle, R.J.; Cho, H. Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1. J. Cell Sci. 2010, 123, 619-626.
237. Tanaka, A.; Cleland, M.M.; Xu, S.; Narendra, D.P.; Suen, D.F.; Karbowski, M.; Youle, R.J. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J. Cell Biol. 2010, 191, 1367-1380.
238. Heo, J.M.; Livnat-Levanon, N.; Taylor, E.B.; Jones, K.T.; Dephoure, N.; Ring, J.; Xie, J.; Brodsky, J.L.; Madeo, F.; Gygi, S.P.; et al. A stress-responsive system for mitochondrial protein degradation. Mol. Cell 2010, 40, 465-480.
239. Xu, S.; Peng, G.; Wang, Y.; Fang, S.; Karbowski, M. The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover. Mol. Biol. Cell 2011, 22, 291-300.
240. Karbowski, M.; Youle, R.J. Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation. Curr. Opin. Cell Biol. 2011, 23, 476-482.
241. Chai, Y.; Koppenhafer, S.L.; Shoesmith, S.J.; Perez, M.K.; Paulson, H.L. Evidence for proteasome involvement in polyglutamine disease: Localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum. Mol. Genet. 1999, 8, 673-682.
242. Shaw, B.F.; Valentine, J.S. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem. Sci. 2007, 32, 78-85.
243. Sugiura, A.; Yonashiro, R.; Fukuda, T.; Matsushita, N.; Nagashima, S.; Inatome, R.; Yanagi, S. A mitochondrial ubiquitin ligase MITOL controls cell toxicity of polyglutamine-expanded protein. Mitochondrion 2011, 11, 139-146.
244. Yonashiro, R.; Sugiura, A.; Miyachi, M.; Fukuda, T.; Matsushita, N.; Inatome, R.; Ogata, Y.; Suzuki, T.; Dohmae, N.; Yanagi, S. Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation. Mol. Biol. Cell 2009, 20, 4524-4530.
245. Scott, I. The role of mitochondria in the mammalian antiviral defense system. Mitochondrion 2010, 10, 316-320.
246. Tal, M.C.; Iwasaki, A. Mitoxosome: A mitochondrial platform for cross-talk between cellular stress and antiviral signaling. Immunol. Rev. 2011, 243, 215-234.
247. Shi, H.X.; Liu, X.; Wang, Q.; Tang, P.P.; Liu, X.Y.; Shan, Y.F.; Wang, C. Mitochondrial ubiquitin ligase MARCH5 promotes TLR7 signaling by attenuating TANK action. PLoS Pathog. 2011, 7, e1002057.
248. Braschi, E.; Zunino, R.; McBride, H.M. MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission. EMBO Rep. 2009, 10, 748-754.
249. Neuspiel, M.; Schauss, A.C.; Braschi, E.; Zunino, R.; Rippstein, P.; Rachubinski, R.A.; Andrade-Navarro, M.A.; McBride, H.M. Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers. Curr. Biol. 2008, 18, 102-108.
250. Braschi, E.; Goyon, V.; Zunino, R.; Mohanty, A.; Xu, L.; McBride, H.M. Vps35 mediates vesicle transport between the mitochondria and peroxisomes. Curr. Biol. 2010, 20, 1310-1315.
251. Youle, R.J.; Narendra, D.P. Mechanisms of mitophagy. Nat. Rev. Mol. Cell Biol. 2011, 12, 9-14.
252. Ziviani, E.; Tao, R.N.; Whitworth, A.J. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. USA 2010, 107, 5018-5023.
253. Poole, A.C.; Thomas, R.E.; Yu, S.; Vincow, E.S.; Pallanck, L. The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway. PLoS One 2010, 5, e10054.
254. Gegg, M.E.; Cooper, J.M.; Chau, K.Y.; Rojo, M.; Schapira, A.H.; Taanman, J.W. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum. Mol. Genet. 2010, 19, 4861-4870.
255. Geisler, S.; Holmstrom, K.M.; Skujat, D.; Fiesel, F.C.; Rothfuss, O.C.; Kahle, P.J.; Springer, W. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat. Cell Biol. 2010, 12, 119-131.
256. Tang, F.; Wang, B.; Li, N.; Wu, Y.; Jia, J.; Suo, T.; Chen, Q.; Liu, Y.J.; Tang, J. RNF185, a Novel Mitochondrial Ubiquitin E3 Ligase, Regulates Autophagy through Interaction with BNIP1. PLoS One 2011, 6, e24367.
257. Guais, A.; Solhonne, B.; Melaine, N.; Guellaen, G.; Bulle, F. Goliath, a ring-H2 mitochondrial protein, regulated by luteinizing hormone/human chorionic gonadotropin in rat leydig cells. Biol. Reprod. 2004, 70, 204-213.