유비퀴틴 C

Ubiquitin C
UBC
Protein UBC PDB 1aar.png
사용 가능한 구조물
PDB직교 검색: PDBe RCSB
식별자
별칭UBC, HMG20, 유비쿼터스 C
외부 IDOMIM: 191340 MGI: 98889 HomoloGene: 128418 GeneCard: UBC
직교체
종인간마우스
엔트레스

7316

22190

앙상블

ENSG00000150991

ENSMUSG00000008348

유니프로트

P0CG48

P0CG50

RefSeq(mRNA)

NM_021009

NM_019639

RefSeq(단백질)

NP_066289

NP_062613

위치(UCSC)Chr 12: 124.91 – 124.92MbCr 5: 125.46 – 125.47Mb
PubMed 검색[3][4]
위키다타
인간 보기/편집마우스 보기/편집

Polyubiquitin-C는 인간의 UBC 유전자에 의해 암호화된 단백질이다.[5][6][7]Polyubiquitin-C는 UBB, UBA52, RPS27A와 함께 유비퀴틴의 원천 중 하나이다.[8]

UBC유전자(UBC유전자)는 포유류에서 스트레스 조절형 폴리우비퀴틴유전자(UBB, UBC) 2종 중 하나이다.그것은 스트레스 조건 하에서 세포의 유비퀴틴 수준을 유지하는 데 핵심적인 역할을 한다.[9][10]UBC 유전자의 결함은 중간 위치 배아 치사성으로 이어질 수 있다.

구조

유전자

UBC 유전자는 12q24.3 염색체에 위치하며, 2개의 exon으로 구성되어 있다.UBC 유전자의 촉진자는 스트레스 시 UBC 유도를 매개하는 Putterative Heat Shock Elements(HSE)를 포함한다.UBC 유전자는 그들이 포함하는 Ub 코딩 단위 수에서 UBB 유전자와 다르다.[9]UBC 유전자에 9~10개의 Ub 단위가 들어 있었다.

단백질

Polyubiquitin-C에서, 주어진 유비퀴틴 분자의 C-terminus는 N-terminal 잔여물 또는 다른 유비퀴틴 분자의 7개 리신 잔류물 중 하나에 공칭적으로 결합된다.[11]유비퀴틴 체인의 서로 다른 연결은 뚜렷한 순응을 낳는다.Polyubiquitin-C에는 8가지 연결 유형이 있으며, 각 유형에는 연결 의존적 역학 및 연결 고유 순응이 있다.[12][13]

함수

폴리우비퀴틴-C의 다양성은 유비쿼터스화가 많은 세포사건의 규제에 기여한다는 것을 의미한다.Polyubiquitin-C는 열충격 반응을 활성화하지 않지만 반응을 유지하는 데 핵심적인 역할을 한다.UBC 유전자 전사는 스트레스 중에 유도되며 손상되거나 접히지 않은 단백질을 제거하는 데 필요한 추가 유비퀴틴을 제공한다.[10][14]Polyubiquitin-C는 선천적 면역, DNA 수리, 키나아제 활동과 같은 다양한 생물학적 과정에 중요한 역할을 한다.[15][16][17]부착되지 않은 폴리우비퀴틴-C 역시 독성 단백질 골재를 제거하기 위해 프로테아솜과 자가포진을 연결하고 조정하는 핵심 신호 분자다.[18]

임상적 유의성

단일 UBC alle의 상실은 명백한 표현형태를 가지고 있지 않은 반면, UBC 유전자의 동질적 삭제는 태아 간 발달의 결함으로 인한 중간 위치 배아 치사성으로 이어지며, 세포 주기 진행의 지연과 세포 스트레스에 대한 민감성 증가로 이어진다.[10]생쥐 배아 섬유질에서 UBC 유전자를 균질하게 삭제하면 산화스트레스에 따른 세포 Ub 수준 저하와 생존성 저하를 초래할 것이라는 보고도 있다.[19]

상호작용

Polyubiquitin-C는 다음과 상호작용하는 것으로 나타났다.

참조

  1. ^ a b c GRCh38: 앙상블 릴리스 89: ENSG00000150991 - 앙상블, 2017년 5월
  2. ^ a b c GRCm38: 앙상블 릴리스 89: ENSMUSG00000008348 - 앙상블, 2017년 5월
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Board PG, Coggan M, Baker RT, Vuust J, Webb GC (April 1992). "Localization of the human UBC polyubiquitin gene to chromosome band 12q24.3". Genomics. 12 (4): 639–42. doi:10.1016/0888-7543(92)90287-3. PMID 1315303.
  6. ^ Marinovic AC, Zheng B, Mitch WE, Price SR (May 2002). "Ubiquitin (UbC) expression in muscle cells is increased by glucocorticoids through a mechanism involving Sp1 and MEK1". The Journal of Biological Chemistry. 277 (19): 16673–81. doi:10.1074/jbc.M200501200. PMID 11872750.
  7. ^ "Entrez Gene: UBC ubiquitin C".
  8. ^ Kimura Y, Tanaka K (June 2010). "Regulatory mechanisms involved in the control of ubiquitin homeostasis". Journal of Biochemistry. 147 (6): 793–8. doi:10.1093/jb/mvq044. PMID 20418328.
  9. ^ a b Wiborg O, Pedersen MS, Wind A, Berglund LE, Marcker KA, Vuust J (March 1985). "The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences". The EMBO Journal. 4 (3): 755–9. doi:10.1002/j.1460-2075.1985.tb03693.x. PMC 554252. PMID 2988935.
  10. ^ a b c Ryu KY, Maehr R, Gilchrist CA, Long MA, Bouley DM, Mueller B, Ploegh HL, Kopito RR (June 2007). "The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress tolerance". The EMBO Journal. 26 (11): 2693–706. doi:10.1038/sj.emboj.7601722. PMC 1888680. PMID 17491588.
  11. ^ Komander D, Rape M (2012). "The ubiquitin code". Annual Review of Biochemistry. 81: 203–29. doi:10.1146/annurev-biochem-060310-170328. PMID 22524316.
  12. ^ Ye Y, Blaser G, Horrocks MH, Ruedas-Rama MJ, Ibrahim S, Zhukov AA, Orte A, Klenerman D, Jackson SE, Komander D (December 2012). "Ubiquitin chain conformation regulates recognition and activity of interacting proteins". Nature. 492 (7428): 266–70. Bibcode:2012Natur.492..266Y. doi:10.1038/nature11722. PMC 3605796. PMID 23201676.
  13. ^ Castañeda CA, Kashyap TR, Nakasone MA, Krueger S, Fushman D (July 2013). "Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains". Structure. 21 (7): 1168–81. doi:10.1016/j.str.2013.04.029. PMC 3802530. PMID 23823328.
  14. ^ Tsirigotis M, Zhang M, Chiu RK, Wouters BG, Gray DA (December 2001). "Sensitivity of mammalian cells expressing mutant ubiquitin to protein-damaging agents". The Journal of Biological Chemistry. 276 (49): 46073–8. doi:10.1074/jbc.M109023200. PMID 11598140.
  15. ^ Rajsbaum R, Versteeg GA, Schmid S, Maestre AM, Belicha-Villanueva A, Martínez-Romero C, Patel JR, Morrison J, Pisanelli G, Miorin L, Laurent-Rolle M, Moulton HM, Stein DA, Fernandez-Sesma A, tenOever BR, García-Sastre A (June 2014). "Unanchored K48-linked polyubiquitin synthesized by the E3-ubiquitin ligase TRIM6 stimulates the interferon-IKKε kinase-mediated antiviral response". Immunity. 40 (6): 880–95. doi:10.1016/j.immuni.2014.04.018. PMC 4114019. PMID 24882218.
  16. ^ Rajsbaum R, García-Sastre A (October 2014). "Virology. Unanchored ubiquitin in virus uncoating". Science. 346 (6208): 427–8. doi:10.1126/science.1261509. PMID 25342790. S2CID 28504276.
  17. ^ Pickart CM, Fushman D (December 2004). "Polyubiquitin chains: polymeric protein signals". Current Opinion in Chemical Biology. 8 (6): 610–6. doi:10.1016/j.cbpa.2004.09.009. PMID 15556404.
  18. ^ Hao R, Nanduri P, Rao Y, Panichelli RS, Ito A, Yoshida M, Yao TP (September 2013). "Proteasomes activate aggresome disassembly and clearance by producing unanchored ubiquitin chains". Molecular Cell. 51 (6): 819–28. doi:10.1016/j.molcel.2013.08.016. PMC 3791850. PMID 24035499.
  19. ^ Ryu HW, Ryu KY (January 2011). "Quantification of oxidative stress in live mouse embryonic fibroblasts by monitoring the responses of polyubiquitin genes". Biochemical and Biophysical Research Communications. 404 (1): 470–5. doi:10.1016/j.bbrc.2010.12.004. PMID 21144824.
  20. ^ a b Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J, Gillard JW, Jaquith JB, Morris SJ, Barker PA (June 2008). "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Molecular Cell. 30 (6): 689–700. doi:10.1016/j.molcel.2008.05.014. PMID 18570872.
  21. ^ Didelot C, Lanneau D, Brunet M, Bouchot A, Cartier J, Jacquel A, Ducoroy P, Cathelin S, Decologne N, Chiosis G, Dubrez-Daloz L, Solary E, Garrido C (May 2008). "Interaction of heat-shock protein 90 beta isoform (HSP90 beta) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiation". Cell Death and Differentiation. 15 (5): 859–66. doi:10.1038/cdd.2008.5. PMID 18239673.
  22. ^ Sekine K, Takubo K, Kikuchi R, Nishimoto M, Kitagawa M, Abe F, Nishikawa K, Tsuruo T, Naito M (April 2008). "Small molecules destabilize cIAP1 by activating auto-ubiquitylation". The Journal of Biological Chemistry. 283 (14): 8961–8. doi:10.1074/jbc.M709525200. PMID 18230607.
  23. ^ Wang WJ, Li QQ, Xu JD, Cao XX, Li HX, Tang F, Chen Q, Yang JM, Xu ZD, Liu XP (2008). "Interaction between CD147 and P-glycoprotein and their regulation by ubiquitination in breast cancer cells". Chemotherapy. 54 (4): 291–301. doi:10.1159/000151225. PMID 18689982. S2CID 7260048.
  24. ^ a b c Tan F, Lu L, Cai Y, Wang J, Xie Y, Wang L, Gong Y, Xu BE, Wu J, Luo Y, Qiang B, Yuan J, Sun X, Peng X (July 2008). "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells". Proteomics. 8 (14): 2885–96. doi:10.1002/pmic.200700887. PMID 18655026. S2CID 25586938.
  25. ^ Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP (October 2011). "Systematic and quantitative assessment of the ubiquitin-modified proteome". Molecular Cell. 44 (2): 325–40. doi:10.1016/j.molcel.2011.08.025. PMC 3200427. PMID 21906983.
  26. ^ Zhou F, Zhang L, Wang A, Song B, Gong K, Zhang L, Hu M, Zhang X, Zhao N, Gong Y (May 2008). "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". The Journal of Biological Chemistry. 283 (21): 14506–15. doi:10.1074/jbc.M706136200. PMID 18367454.
  27. ^ a b Sehat B, Andersson S, Girnita L, Larsson O (July 2008). "Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis". Cancer Research. 68 (14): 5669–77. doi:10.1158/0008-5472.CAN-07-6364. PMID 18632619.
  28. ^ Pennock S, Wang Z (May 2008). "A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation". Molecular and Cellular Biology. 28 (9): 3020–37. doi:10.1128/MCB.01809-07. PMC 2293090. PMID 18316398.
  29. ^ Umebayashi K, Stenmark H, Yoshimori T (August 2008). "Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation". Molecular Biology of the Cell. 19 (8): 3454–62. doi:10.1091/mbc.E07-10-0988. PMC 2488299. PMID 18508924.
  30. ^ André H, Pereira TS (October 2008). "Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha". The Journal of Biological Chemistry. 283 (43): 29375–84. doi:10.1074/jbc.M805919200. PMC 2662024. PMID 18694926.
  31. ^ Park YK, Ahn DR, Oh M, Lee T, Yang EG, Son M, Park H (July 2008). "Nitric oxide donor, (+/-)-S-nitroso-N-acetylpenicillamine, stabilizes transactive hypoxia-inducible factor-1alpha by inhibiting von Hippel-Lindau recruitment and asparagine hydroxylation". Molecular Pharmacology. 74 (1): 236–45. doi:10.1124/mol.108.045278. PMID 18426857. S2CID 31675735.
  32. ^ Kim BY, Kim H, Cho EJ, Youn HD (February 2008). "Nur77 upregulates HIF-alpha by inhibiting pVHL-mediated degradation". Experimental & Molecular Medicine. 40 (1): 71–83. doi:10.3858/emm.2008.40.1.71. PMC 2679322. PMID 18305400.
  33. ^ a b c Newton K, Matsumoto ML, Wertz IE, Kirkpatrick DS, Lill JR, Tan J, Dugger D, Gordon N, Sidhu SS, Fellouse FA, Komuves L, French DM, Ferrando RE, Lam C, Compaan D, Yu C, Bosanac I, Hymowitz SG, Kelley RF, Dixit VM (August 2008). "Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies". Cell. 134 (4): 668–78. doi:10.1016/j.cell.2008.07.039. PMID 18724939. S2CID 3955385.
  34. ^ a b Conze DB, Wu CJ, Thomas JA, Landstrom A, Ashwell JD (May 2008). "Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation". Molecular and Cellular Biology. 28 (10): 3538–47. doi:10.1128/MCB.02098-07. PMC 2423148. PMID 18347055.
  35. ^ Xiao H, Qian W, Staschke K, Qian Y, Cui G, Deng L, Ehsani M, Wang X, Qian YW, Chen ZJ, Gilmour R, Jiang Z, Li X (May 2008). "Pellino 3b negatively regulates interleukin-1-induced TAK1-dependent NF kappaB activation". The Journal of Biological Chemistry. 283 (21): 14654–64. doi:10.1074/jbc.M706931200. PMC 2386918. PMID 18326498.
  36. ^ Windheim M, Stafford M, Peggie M, Cohen P (March 2008). "Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptor-associated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase". Molecular and Cellular Biology. 28 (5): 1783–91. doi:10.1128/MCB.02380-06. PMC 2258775. PMID 18180283.
  37. ^ KIAA0753 Gene - GeneCards K0753 단백질 K0753 항체(https://www.genecards.org/cgi-bin/carddisp.pl?gene=KIAA0753)에서 구입 가능).
  38. ^ a b Al-Hakim AK, Zagorska A, Chapman L, Deak M, Peggie M, Alessi DR (April 2008). "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains" (PDF). The Biochemical Journal. 411 (2): 249–60. doi:10.1042/BJ20080067. PMID 18254724.
  39. ^ a b Ivanchuk SM, Mondal S, Rutka JT (June 2008). "p14ARF interacts with DAXX: effects on HDM2 and p53". Cell Cycle. 7 (12): 1836–50. doi:10.4161/cc.7.12.6025. PMID 18583933.
  40. ^ a b Song MS, Song SJ, Kim SY, Oh HJ, Lim DS (July 2008). "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex". The EMBO Journal. 27 (13): 1863–74. doi:10.1038/emboj.2008.115. PMC 2486425. PMID 18566590.
  41. ^ a b Yang W, Dicker DT, Chen J, El-Deiry WS (March 2008). "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2". Cell Cycle. 7 (5): 670–82. doi:10.4161/cc.7.5.5701. PMID 18382127.
  42. ^ Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C (October 2011). "A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles". Molecular & Cellular Proteomics. 10 (10): M111.013284. doi:10.1074/mcp.M111.013284. PMC 3205876. PMID 21890473.
  43. ^ Shibata T, Ohta T, Tong KI, Kokubu A, Odogawa R, Tsuta K, Asamura H, Yamamoto M, Hirohashi S (September 2008). "Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy". Proceedings of the National Academy of Sciences of the United States of America. 105 (36): 13568–73. Bibcode:2008PNAS..10513568S. doi:10.1073/pnas.0806268105. PMC 2533230. PMID 18757741.
  44. ^ Patel R, Maru G (June 2008). "Polymeric black tea polyphenols induce phase II enzymes via Nrf2 in mouse liver and lungs". Free Radical Biology & Medicine. 44 (11): 1897–911. doi:10.1016/j.freeradbiomed.2008.02.006. PMID 18358244.
  45. ^ Chastagner P, Israël A, Brou C (2008). Wölfl S (ed.). "AIP4/Itch regulates Notch receptor degradation in the absence of ligand". PLOS ONE. 3 (7): e2735. Bibcode:2008PLoSO...3.2735C. doi:10.1371/journal.pone.0002735. PMC 2444042. PMID 18628966.
  46. ^ Li JG, Haines DS, Liu-Chen LY (April 2008). "Agonist-promoted Lys63-linked polyubiquitination of the human kappa-opioid receptor is involved in receptor down-regulation". Molecular Pharmacology. 73 (4): 1319–30. doi:10.1124/mol.107.042846. PMC 3489932. PMID 18212250.
  47. ^ Han JM, Park BJ, Park SG, Oh YS, Choi SJ, Lee SW, Hwang SK, Chang SH, Cho MH, Kim S (August 2008). "AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53". Proceedings of the National Academy of Sciences of the United States of America. 105 (32): 11206–11. Bibcode:2008PNAS..10511206H. doi:10.1073/pnas.0800297105. PMC 2516205. PMID 18695251.
  48. ^ Abe Y, Oda-Sato E, Tobiume K, Kawauchi K, Taya Y, Okamoto K, Oren M, Tanaka N (March 2008). "Hedgehog signaling overrides p53-mediated tumor suppression by activating Mdm2". Proceedings of the National Academy of Sciences of the United States of America. 105 (12): 4838–43. Bibcode:2008PNAS..105.4838A. doi:10.1073/pnas.0712216105. PMC 2290789. PMID 18359851.
  49. ^ Zhang Z, Zhang R (March 2008). "Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation". The EMBO Journal. 27 (6): 852–64. doi:10.1038/emboj.2008.25. PMC 2265109. PMID 18309296.
  50. ^ Dohmesen C, Koeppel M, Dobbelstein M (January 2008). "Specific inhibition of Mdm2-mediated neddylation by Tip60". Cell Cycle. 7 (2): 222–31. doi:10.4161/cc.7.2.5185. PMID 18264029.
  51. ^ Motegi A, Liaw HJ, Lee KY, Roest HP, Maas A, Wu X, Moinova H, Markowitz SD, Ding H, Hoeijmakers JH, Myung K (August 2008). "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks". Proceedings of the National Academy of Sciences of the United States of America. 105 (34): 12411–6. Bibcode:2008PNAS..10512411M. doi:10.1073/pnas.0805685105. PMC 2518831. PMID 18719106.
  52. ^ Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L (March 2008). "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination". Proceedings of the National Academy of Sciences of the United States of America. 105 (10): 3768–73. Bibcode:2008PNAS..105.3768U. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726.
  53. ^ Brun J, Chiu R, Lockhart K, Xiao W, Wouters BG, Gray DA (2008). "hMMS2 serves a redundant role in human PCNA polyubiquitination". BMC Molecular Biology. 9: 24. doi:10.1186/1471-2199-9-24. PMC 2263069. PMID 18284681.
  54. ^ Yu F, Zhou J (July 2008). "Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress". Neuroscience Letters. 440 (1): 4–8. doi:10.1016/j.neulet.2008.05.052. PMID 18541373. S2CID 2169911.
  55. ^ Kawahara K, Hashimoto M, Bar-On P, Ho GJ, Crews L, Mizuno H, Rockenstein E, Imam SZ, Masliah E (March 2008). "alpha-Synuclein aggregates interfere with Parkin solubility and distribution: role in the pathogenesis of Parkinson disease". The Journal of Biological Chemistry. 283 (11): 6979–87. doi:10.1074/jbc.M710418200. PMID 18195004.
  56. ^ a b Ma Q, Zhou L, Shi H, Huo K (June 2008). "NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation". Cellular Signalling. 20 (6): 1044–51. doi:10.1016/j.cellsig.2008.01.015. PMID 18299187.
  57. ^ Varfolomeev E, Goncharov T, Fedorova AV, Dynek JN, Zobel K, Deshayes K, Fairbrother WJ, Vucic D (September 2008). "c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation". The Journal of Biological Chemistry. 283 (36): 24295–9. doi:10.1074/jbc.C800128200. PMC 3259840. PMID 18621737.
  58. ^ Liao W, Xiao Q, Tchikov V, Fujita K, Yang W, Wincovitch S, Garfield S, Conze D, El-Deiry WS, Schütze S, Srinivasula SM (May 2008). "CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation". Current Biology. 18 (9): 641–9. doi:10.1016/j.cub.2008.04.017. PMC 2587165. PMID 18450452.
  59. ^ Panasyuk G, Nemazanyy I, Filonenko V, Gout I (May 2008). "Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1". Biochemical and Biophysical Research Communications. 369 (2): 339–43. doi:10.1016/j.bbrc.2008.02.016. PMID 18279656.
  60. ^ He KL, Deora AB, Xiong H, Ling Q, Weksler BB, Niesvizky R, Hajjar KA (July 2008). "Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11". The Journal of Biological Chemistry. 283 (28): 19192–200. doi:10.1074/jbc.M800100200. PMC 2443646. PMID 18434302.
  61. ^ a b Boulkroun S, Ruffieux-Daidié D, Vitagliano JJ, Poirot O, Charles RP, Lagnaz D, Firsov D, Kellenberger S, Staub O (October 2008). "Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3". American Journal of Physiology. Renal Physiology. 295 (4): F889–900. doi:10.1152/ajprenal.00001.2008. PMID 18632802.
  62. ^ a b Raikwar NS, Thomas CP (May 2008). "Nedd4-2 isoforms ubiquitinate individual epithelial sodium channel subunits and reduce surface expression and function of the epithelial sodium channel". American Journal of Physiology. Renal Physiology. 294 (5): F1157–65. doi:10.1152/ajprenal.00339.2007. PMC 2424110. PMID 18322022.
  63. ^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  64. ^ Stolfi C, Fina D, Caruso R, Caprioli F, Fantini MC, Rizzo A, Sarra M, Pallone F, Monteleone G (June 2008). "Mesalazine negatively regulates CDC25A protein expression and promotes accumulation of colon cancer cells in S phase". Carcinogenesis. 29 (6): 1258–66. doi:10.1093/carcin/bgn122. PMID 18495657.
  65. ^ Guo X, Ramirez A, Waddell DS, Li Z, Liu X, Wang XF (January 2008). "Axin and GSK3- control Smad3 protein stability and modulate TGF- signaling". Genes & Development. 22 (1): 106–20. doi:10.1101/gad.1590908. PMC 2151009. PMID 18172167.
  66. ^ Carpentier I, Coornaert B, Beyaert R (October 2008). "Smurf2 is a TRAF2 binding protein that triggers TNF-R2 ubiquitination and TNF-R2-induced JNK activation". Biochemical and Biophysical Research Communications. 374 (4): 752–7. doi:10.1016/j.bbrc.2008.07.103. PMID 18671942.
  67. ^ Lee YS, Han JM, Son SH, Choi JW, Jeon EJ, Bae SC, Park YI, Kim S (July 2008). "AIMP1/p43 downregulates TGF-beta signaling via stabilization of smurf2". Biochemical and Biophysical Research Communications. 371 (3): 395–400. doi:10.1016/j.bbrc.2008.04.099. PMID 18448069.
  68. ^ Wang YT, Chuang JY, Shen MR, Yang WB, Chang WC, Hung JJ (July 2008). "Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process". Journal of Molecular Biology. 380 (5): 869–85. doi:10.1016/j.jmb.2008.05.043. PMID 18572193.
  69. ^ Chen L, Dong W, Zou T, Ouyang L, He G, Liu Y, Qi Y (August 2008). "Protein phosphatase 4 negatively regulates LPS cascade by inhibiting ubiquitination of TRAF6". FEBS Letters. 582 (19): 2843–9. doi:10.1016/j.febslet.2008.07.014. PMID 18634786. S2CID 27700566.
  70. ^ Lamothe B, Campos AD, Webster WK, Gopinathan A, Hur L, Darnay BG (September 2008). "The RING domain and first zinc finger of TRAF6 coordinate signaling by interleukin-1, lipopolysaccharide, and RANKL". The Journal of Biological Chemistry. 283 (36): 24871–80. doi:10.1074/jbc.M802749200. PMC 2529010. PMID 18617513.

추가 읽기