Mdm2

MDM2
מבנים זמינים
בנק מידע החלבונים	חיפוש אורתולוגים: PDBe RCSB
רשימת מבנים
	1RV1, 1T4E, 1T4F, 1YCR, 1Z1M, 2AXI, 2C6A, 2C6B, 2FOP, 2GV2, 2HDP, 2LZG, 2M86, 2MPS, 2RUH, 2VJE, 2VJF, 3EQS, 3G03, 3IUX, 3IWY, 3JZK, 3JZR, 3JZS, 3LBK, 3LBL, 3LNJ, 3LNZ, 3MQS, 3TJ2, 3TPX, 3TU1, 3V3B, 3VBG, 3VZV, 3W69, 4DIJ, 4ERE, 4ERF, 4HBM, 4HFZ, 4HG7, 4JV7, 4JV9, 4JVE, 4JVR, 4JWR, 4MDN, 4MDQ, 4OAS, 4OBA, 4OCC, 4ODE, 4ODF, 4OGN, 4OGT, 4OGV, 4OQ3, 4QO4, 4QOC, 4UMN, 4WT2, 4XXB, 4ZYC, 4ZYF, 4ZYI, 4UE1, 4UD7, 5AFG, 5HMI, 5HMK, 5HMH, 5C5A
מזהים
שמות נוספים	MDM2, ACTFS, HDMX, hdm2, MDM2 proto-oncogene, LSKB
מזהים חיצוניים	OMIM: 164785 MGI: 96952 HomoloGene: 1793 GeneCards: MDM2
מיקום הגן (באדם)
כרומוזום	כרומוזום 12
סוף	68,845,544 bp
מיקום הגן (בעכבר)
כרומוזום	כרומוזום 10 (בעכבר)
סוף	117,546,663 bp
תבנית ביטוי RNA
	; ; ; ;
	נתוני התבטאות נוספים
אונטולוגיית גנים (GO)
תפקיד מולקולרי	• scaffold protein binding; • GO:0001948, GO:0016582 קשירת חלבונים; • enzyme binding; • קשירת יוני מתכת; • קשירת חלבון דומה; • UB; • p53 binding; • SUMO transferase activity; • GO:0050372 ubiquitin-protein transferase activity; • פעילות טרנספראז; • ligase activity; • 5S rRNA binding; • zinc ion binding; • ribonucleoprotein complex binding; • protein N-terminus binding; • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity; • NEDD8 ligase activity; • disordered domain specific binding; • protein domain specific binding; • receptor serine/threonine kinase binding; • peroxisome proliferator activated receptor binding; • ubiquitin binding;
מיקום בתא	• ציטוזול; • endocytic vesicle membrane; • קרום התא; • סינפסה; • nuclear body; • ציטופלזמה; • גרעין התא; • נוקלאופלזמה; • גרעינון; • GO:0009327 מבנה מקרומולקולרי;
תהליכים ביולוגיים	• negative regulation of signal transduction by p53 class mediator; • endocardial cushion morphogenesis; • cellular response to UV-C; • atrial septum development; • regulation of heart rate; • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; • GO:1901313 בקרה חיובית של ביטוי גנים; • blood vessel development; • בקרה חיובית של שגשוג תאים; • negative regulation of DNA damage response, signal transduction by p53 class mediator; • response to ether; • blood vessel remodeling; • תגובה תאית להיפוקסיה; • heart valve development; • cellular response to estrogen stimulus; • בקרה שלילית של תהליך אפופטוזה; • cellular response to organic substance; • cellular response to hydrogen peroxide; • response to cocaine; • cardiac septum morphogenesis; • GO:1901227 negative regulation of transcription by RNA polymerase II; • GO:0018054 peptidyl-lysine modification; • positive regulation of cell cycle; • ventricular septum development; • positive regulation of protein export from nucleus; • response to steroid hormone; • cellular response to growth factor stimulus; • GO:1903362 regulation of protein catabolic process; • GO:1904577 cellular response to antibiotic; • negative regulation of gene expression; • positive regulation of mitotic cell cycle; • heart development; • cellular response to alkaloid; • cellular response to vitamin B1; • response to magnesium ion; • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; • positive regulation of proteasomal ubiquitin-dependent protein catabolic process; • cellular response to peptide hormone stimulus; • GO:1904579 cellular response to organic cyclic compound; • GO:0022415 viral process; • response to iron ion; • בקרת גנים; • GO:1904576 response to antibiotic; • traversing start control point of mitotic cell cycle; • protein ubiquitination; • negative regulation of protein processing; • establishment of protein localization; • response to toxic substance; • response to morphine; • atrioventricular valve morphogenesis; • protein localization to nucleus; • regulation of signal transduction by p53 class mediator; • positive regulation of vascular associated smooth muscle cell proliferation; • response to water-immersion restraint stress; • negative regulation of neuron projection development; • positive regulation of vascular associated smooth muscle cell migration; • protein deubiquitination; • protein sumoylation; • transcription factor catabolic process; • protein autoubiquitination; • response to formaldehyde; • protein destabilization; • GO:0045996 negative regulation of transcription, DNA-templated; • proteolysis involved in cellular protein catabolic process; • cellular response to gamma radiation; • cellular response to actinomycin D; • negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; • amyloid fibril formation; • GO:0034622 protein-containing complex assembly; • ubiquitin-dependent protein catabolic process;
	מקורות: Amigo / QuickGO
אורתולוגים
	4193
	17246
	ENSG00000135679
	ENSMUSG00000020184
	Q00987
	P23804
NM_001145336; NM_001145337; NM_001145339; NM_001145340; NM_001278462;
	NM_002392; NM_006878; NM_006879; NM_006880; NM_006881; NM_006882; NM_032739; NM_001367990
	NM_001288586; NM_010786
NP_001138809; NP_001138811; NP_001138812; NP_001265391; NP_002383;
	NP_001354919
	NP_001275515; NP_034916
	ויקינתונים
צפייה/עריכה נתוני אדם	צפייה/עריכה נתוני עכבר

MDM2 הוא רגולטור שלילי חשוב של החלבון p53 שמונע גידולים. הוא השם גם של הגן וגם של החלבון שהגן מקדד.

גילוי

האונקוגן שמקדד את החלבון MDM2 שובט לראשונה, ביחד עם הגנים MDM1 ו-MDM3, משורת התאים העכבריים 3T3-DM. ביטוי יתר שלו, יחד עם Ras האונקוגני מניע התמרה של פיברובלסטים עכבריים, וביטוי של MDM2 גורם ליצירת גידולים בעכברים ערומים. לחלבון זה קיים הומולוג אנושי שלפעמים נקרא HDM2. אישוש לכך של-MDM2 יש חלק בהתפתחות גידולים, חוקרים מצאו רמות מוגברות של החלבון בסוגי סרטן מסוימים. MDM4, שלפעמים נקרא MDMX, הוא באותה משפחה של MDM2, וגם לו יש תפקיד כרגולטור שלילי של p53.

אינטראקציות

המחקר הראה ש- MDM2 פועל ביחד עם HDAC1,^[5] RPL26,^[6] FKBP3,^[7] CCNG1,^[8] HTATIP,^[9] GNL3,^[10] Death associated protein 6,^[11] PSME3,^[12] Insulin-like growth factor 1 receptor,^[13] RRM2B,^[14] FOXO4,^[15] Ribosomal protein L5,^[10]^[16]^[17] ABL,^[18] RYBP,^[19] HIF1A,^[20]^[21] PCAF,^[22] TATA binding protein,^[23]^[24] P73,^[25]^[26] CTBP2,^[27] NUMB,^[28]^[29] P53,^[30]^[31] P16,^[11]^[16]^[32]^[33]^[34] PSMD10,^[35] EP300,^[36] CTBP1,^[27] MDM4,^[37]^[38]^[39]^[40] RPL11,^[10]^[16] Promyelocytic leukemia protein,^[41]^[42]^[43]^[44] Dihydrofolate reductase,^[45] Arrestin beta 2,^[46]^[47]^[48] Arrestin beta 1^[47]^[48] ו־Ubiquitin C.^[11]^[49]^[50]

ראו גם

לקריאה נוספת

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Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM (במרץ 2000). "Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53". J. Biol. Chem. 275 (12): 8945–51. doi:10.1074/jbc.275.12.8945. PMID 10722742. אורכב מ-המקור ב-2019-12-16. נבדק ב-2012-08-27. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
Freedman DA, Wu L, Levine AJ (בינואר 1999). "Functions of the MDM2 oncoprotein". Cell. Mol. Life Sci. 55 (1): 96–107. doi:10.1007/s000180050273. PMID 10065155. אורכב מ-המקור ב-2000-06-22. נבדק ב-2012-08-27. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
Hay TJ, Meek DW (ביולי 2000). "Multiple sites of in vivo phosphorylation in the MDM2 oncoprotein cluster within two important functional domains". FEBS Lett. 478 (1–2): 183–6. doi:10.1016/S0014-5793(00)01850-0. PMID 10922493. {{cite journal}}: (עזרה)
Honda, R; Tanaka, H; Yasuda, H (בדצמבר 1997). "Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53". FEBS Lett. 420 (1): 25–7. doi:10.1016/S0014-5793(97)01480-4. PMID 9450543. {{cite journal}}: (עזרה)
Honda R, Yasuda H (במרץ 2000). "Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase". Oncogene. 19 (11): 1473–6. doi:10.1038/sj.onc.1203464. PMID 10723139. {{cite journal}}: (עזרה)
Kubbutat MH, Jones SN, Vousden KH (במאי 1997). "Regulation of p53 stability by Mdm2". Nature. 387 (6630): 299–303. doi:10.1038/387299a0. PMID 9153396. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
Kussie PH, Gorina S, Marechal V (בנובמבר 1996). "Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain". Science. 274 (5289): 948–53. doi:10.1126/science.274.5289.948. PMID 8875929. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
Meek DW, Knippschild U (בדצמבר 2003). "Posttranslational modification of MDM2". Mol. Cancer Res. 1 (14): 1017–26. PMID 14707285. {{cite journal}}: (עזרה)
Midgley CA, Desterro JM, Saville MK (במאי 2000). "An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo". Oncogene. 19 (19): 2312–23. doi:10.1038/sj.onc.1203593. PMID 10822382. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
Momand J, Wu HH, Dasgupta G (בינואר 2000). "MDM2--master regulator of the p53 tumor suppressor protein". Gene. 242 (1–2): 15–29. doi:10.1016/S0378-1119(99)00487-4. PMID 10721693. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
Momand J, Zambetti GP, Olson DC, George D, Levine AJ (ביוני 1992). "The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation". Cell. 69 (7): 1237–45. doi:10.1016/0092-8674(92)90644-R. PMID 1535557. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
Shieh SY, Ikeda M, Taya Y, Prives C (באוקטובר 1997). "DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2". Cell. 91 (3): 325–34. doi:10.1016/S0092-8674(00)80416-X. PMID 9363941. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
Tao W, Levine AJ (ביוני 1999). "P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2". Proc. Natl. Acad. Sci. U.S.A. 96 (12): 6937–41. doi:10.1073/pnas.96.12.6937. PMC 22020. PMID 10359817. {{cite journal}}: (עזרה)
Tao W, Levine AJ (במרץ 1999). "Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53". Proc. Natl. Acad. Sci. U.S.A. 96 (6): 3077–80. doi:10.1073/pnas.96.6.3077. PMC 15897. PMID 10077639. {{cite journal}}: (עזרה)

הערות שוליים

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^ Grossman SR, Perez M, Kung AL (באוקטובר 1998). "p300/MDM2 complexes participate in MDM2-mediated p53 degradation". Mol. Cell. 2 (4): 405–15. doi:10.1016/S1097-2765(00)80140-9. PMID 9809062. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
^ Kadakia, Madhavi; Brown Thomas L; McGorry Molly M; Berberich Steven J (בדצמבר 2002). "MdmX inhibits Smad transactivation". Oncogene. 21 (57): 8776–85. doi:10.1038/sj.onc.1205993. PMID 12483531. {{cite journal}}: (עזרה)
^ Tanimura, S; Ohtsuka S; Mitsui K; Shirouzu K; Yoshimura A; Ohtsubo M (במרץ 1999). "MDM2 interacts with MDMX through their RING finger domains". FEBS Lett. 447 (1): 5–9. doi:10.1016/S0014-5793(99)00254-9. PMID 10218570. {{cite journal}}: (עזרה)
^ Badciong, James C; Haas Arthur L (בדצמבר 2002). "MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination". J. Biol. Chem. 277 (51): 49668–75. doi:10.1074/jbc.M208593200. PMID 12393902. {{cite journal}}: (עזרה)
^ Linke, K; Mace P D; Smith C A; Vaux D L; Silke J; Day C L (במאי 2008). "Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans". Cell Death Differ. 15 (5): 841–8. doi:10.1038/sj.cdd.4402309. PMID 18219319. {{cite journal}}: (עזרה)
^ Bernardi, Rosa; Scaglioni Pier Paolo; Bergmann Stephan; Horn Henning F; Vousden Karen H; Pandolfi Pier Paolo (ביולי 2004). "PML regulates p53 stability by sequestering Mdm2 to the nucleolus". Nat. Cell Biol. 6 (7): 665–72. doi:10.1038/ncb1147. PMID 15195100. {{cite journal}}: (עזרה)
^ Zhu, Hongyan; Wu Liqing; Maki Carl G (בדצמבר 2003). "MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53". J. Biol. Chem. 278 (49): 49286–92. doi:10.1074/jbc.M308302200. PMID 14507915. {{cite journal}}: (עזרה)
^ Kurki S, Latonen L, Laiho M (באוקטובר 2003). "Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization". J. Cell. Sci. 116 (Pt 19): 3917–25. doi:10.1242/jcs.00714. PMID 12915590. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)
^ Wei, Xiaolong; Yu Zhong Kang; Ramalingam Arivudainambi; Grossman Steven R; Yu Jiang H; Bloch Donald B; Maki Carl G (באוגוסט 2003). "Physical and functional interactions between PML and MDM2". J. Biol. Chem. 278 (31): 29288–97. doi:10.1074/jbc.M212215200. PMID 12759344. {{cite journal}}: (עזרה)
^ Maguire, Maria; Nield Paul C; Devling Timothy; Jenkins Rosalind E; Park B Kevin; Polański Radoslaw; Vlatković Nikolina; Boyd Mark T (במאי 2008). "MDM2 regulates dihydrofolate reductase activity through monoubiquitination". Cancer Res. 68 (9): 3232–42. doi:10.1158/0008-5472.CAN-07-5271. PMID 18451149. {{cite journal}}: (עזרה)
^ Wang, Ping; Gao Hua; Ni Yanxiang; Wang Beibei; Wu Yalan; Ji Lili; Qin Linhua; Ma Lan; Pei Gang (בפברואר 2003). "Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2". J. Biol. Chem. 278 (8): 6363–70. doi:10.1074/jbc.M210350200. PMID 12488444. {{cite journal}}: (עזרה)
^ ¹ ² Wang, Ping; Wu Yalan; Ge Xin; Ma Lan; Pei Gang (במרץ 2003). "Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus". J. Biol. Chem. 278 (13): 11648–53. doi:10.1074/jbc.M208109200. PMID 12538596. {{cite journal}}: (עזרה)
^ ¹ ² Shenoy, Sudha K; Xiao Kunhong; Venkataramanan Vidya; Snyder Peter M; Freedman Neil J; Weissman Allan M (באוגוסט 2008). "Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor". J. Biol. Chem. 283 (32): 22166–76. doi:10.1074/jbc.M709668200. PMC 2494938. PMID 18544533. {{cite journal}}: (עזרה)
^ Song, Min Sup; Song Su Jung; Kim So Yeon; Oh Hyun Jung; Lim Dae-Sik (ביולי 2008). "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex". EMBO J. 27 (13): 1863–74. doi:10.1038/emboj.2008.115. PMC 2486425. PMID 18566590. {{cite journal}}: (עזרה)
^ Yang, Wensheng; Dicker David T; Chen Jiandong; El-Deiry Wafik S (במרץ 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. {{cite journal}}: (עזרה)

[refGRCh38Ensembl-1] ¹ ² ³ GRCh38: Ensembl גרסה 89: ENSG00000135679 - Ensembl, מאי 2017

[refGRCm38Ensembl-2] ¹ ² ³ GRCm38: Ensembl גרסה 89: ENSMUSG00000020184 - Ensembl, מאי 2017

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[pmid9529248-34] Pomerantz, J; Schreiber-Agus N; Liégeois N J; Silverman A; Alland L; Chin L; Potes J; Chen K; Orlow I; Lee H W; Cordon-Cardo C; DePinho R A (במרץ 1998). "The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53". Cell. 92 (6): 713–23. doi:10.1016/S0092-8674(00)81400-2. PMID 9529248. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)

[pmid18332869-35] Qiu W, Wu J, Walsh EM (ביולי 2008). "Retinoblastoma protein modulates gankyrin-MDM2 in regulation of p53 stability and chemosensitivity in cancer cells". Oncogene. 27 (29): 4034–43. doi:10.1038/onc.2008.43. PMID 18332869. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)

[pmid9809062-36] Grossman SR, Perez M, Kung AL (באוקטובר 1998). "p300/MDM2 complexes participate in MDM2-mediated p53 degradation". Mol. Cell. 2 (4): 405–15. doi:10.1016/S1097-2765(00)80140-9. PMID 9809062. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)

[pmid12483531-37] Kadakia, Madhavi; Brown Thomas L; McGorry Molly M; Berberich Steven J (בדצמבר 2002). "MdmX inhibits Smad transactivation". Oncogene. 21 (57): 8776–85. doi:10.1038/sj.onc.1205993. PMID 12483531. {{cite journal}}: (עזרה)

[pmid10218570-38] Tanimura, S; Ohtsuka S; Mitsui K; Shirouzu K; Yoshimura A; Ohtsubo M (במרץ 1999). "MDM2 interacts with MDMX through their RING finger domains". FEBS Lett. 447 (1): 5–9. doi:10.1016/S0014-5793(99)00254-9. PMID 10218570. {{cite journal}}: (עזרה)

[pmid12393902-39] Badciong, James C; Haas Arthur L (בדצמבר 2002). "MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination". J. Biol. Chem. 277 (51): 49668–75. doi:10.1074/jbc.M208593200. PMID 12393902. {{cite journal}}: (עזרה)

[pmid18219319-40] Linke, K; Mace P D; Smith C A; Vaux D L; Silke J; Day C L (במאי 2008). "Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans". Cell Death Differ. 15 (5): 841–8. doi:10.1038/sj.cdd.4402309. PMID 18219319. {{cite journal}}: (עזרה)

[pmid15195100-41] Bernardi, Rosa; Scaglioni Pier Paolo; Bergmann Stephan; Horn Henning F; Vousden Karen H; Pandolfi Pier Paolo (ביולי 2004). "PML regulates p53 stability by sequestering Mdm2 to the nucleolus". Nat. Cell Biol. 6 (7): 665–72. doi:10.1038/ncb1147. PMID 15195100. {{cite journal}}: (עזרה)

[pmid14507915-42] Zhu, Hongyan; Wu Liqing; Maki Carl G (בדצמבר 2003). "MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53". J. Biol. Chem. 278 (49): 49286–92. doi:10.1074/jbc.M308302200. PMID 14507915. {{cite journal}}: (עזרה)

[pmid12915590-43] Kurki S, Latonen L, Laiho M (באוקטובר 2003). "Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization". J. Cell. Sci. 116 (Pt 19): 3917–25. doi:10.1242/jcs.00714. PMID 12915590. {{cite journal}}: (עזרה)תחזוקה - ציטוט: multiple names: authors list (link)

[pmid12759344-44] Wei, Xiaolong; Yu Zhong Kang; Ramalingam Arivudainambi; Grossman Steven R; Yu Jiang H; Bloch Donald B; Maki Carl G (באוגוסט 2003). "Physical and functional interactions between PML and MDM2". J. Biol. Chem. 278 (31): 29288–97. doi:10.1074/jbc.M212215200. PMID 12759344. {{cite journal}}: (עזרה)

[pmid18451149-45] Maguire, Maria; Nield Paul C; Devling Timothy; Jenkins Rosalind E; Park B Kevin; Polański Radoslaw; Vlatković Nikolina; Boyd Mark T (במאי 2008). "MDM2 regulates dihydrofolate reductase activity through monoubiquitination". Cancer Res. 68 (9): 3232–42. doi:10.1158/0008-5472.CAN-07-5271. PMID 18451149. {{cite journal}}: (עזרה)

[pmid12488444-46] Wang, Ping; Gao Hua; Ni Yanxiang; Wang Beibei; Wu Yalan; Ji Lili; Qin Linhua; Ma Lan; Pei Gang (בפברואר 2003). "Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2". J. Biol. Chem. 278 (8): 6363–70. doi:10.1074/jbc.M210350200. PMID 12488444. {{cite journal}}: (עזרה)

[pmid12538596-47] ¹ ² Wang, Ping; Wu Yalan; Ge Xin; Ma Lan; Pei Gang (במרץ 2003). "Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus". J. Biol. Chem. 278 (13): 11648–53. doi:10.1074/jbc.M208109200. PMID 12538596. {{cite journal}}: (עזרה)

[pmid18544533-48] ¹ ² Shenoy, Sudha K; Xiao Kunhong; Venkataramanan Vidya; Snyder Peter M; Freedman Neil J; Weissman Allan M (באוגוסט 2008). "Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor". J. Biol. Chem. 283 (32): 22166–76. doi:10.1074/jbc.M709668200. PMC 2494938. PMID 18544533. {{cite journal}}: (עזרה)

[pmid18566590-49] Song, Min Sup; Song Su Jung; Kim So Yeon; Oh Hyun Jung; Lim Dae-Sik (ביולי 2008). "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex". EMBO J. 27 (13): 1863–74. doi:10.1038/emboj.2008.115. PMC 2486425. PMID 18566590. {{cite journal}}: (עזרה)

[pmid18382127-50] Yang, Wensheng; Dicker David T; Chen Jiandong; El-Deiry Wafik S (במרץ 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. {{cite journal}}: (עזרה)

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