Mdm2

MDM2
ساختارهای موجود
PDB	جستجوی هم‌ساخت‌شناسی: PDBe RCSB
فهرست شناسه‌های PDB
	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
معین‌کننده‌ها
نام‌های دیگر	MDM2, ACTFS, HDMX, hdm2, MDM2 proto-oncogene, LSKB
شناسه‌های بیرونی	OMIM: 164785 MGI: 96952 HomoloGene: 1793 GeneCards: MDM2
موقعیت ژن (موش)
کروموزوم	کروموزوم ۱۰ (موش)
پایان	117,546,663 bp
الگوی گسترش RNA
	; ; ; ;
	More reference expression data
هستی‌شناسی ژن
عملکرد ملکولی	• scaffold protein binding; • GO:0001948، GO:0016582 پیوند پروتئینی; • enzyme binding; • metal ion binding; • identical protein binding; • ubiquitin protein ligase binding; • p53 binding; • SUMO transferase activity; • GO:0050372 ubiquitin-protein transferase activity; • transferase activity; • 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;
ترکیبات سلولی	• سیتوزول; • endocytic vesicle membrane; • پوسته یاخته; • سیناپس; • nuclear body; • سیتوپلاسم; • هسته یاخته; • نوکلئوپلاسم; • هستک; • GO:0009327 protein-containing complex;
فرایند زیستی	• 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 positive regulation of gene expression; • blood vessel development; • positive regulation of cell population proliferation; • negative regulation of DNA damage response, signal transduction by p53 class mediator; • response to ether; • blood vessel remodeling; • cellular response to hypoxia; • heart valve development; • cellular response to estrogen stimulus; • negative regulation of apoptotic process; • 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; • ساماندهی بیان ژن; • 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;
	منابع: آمیگو / کوئیک‌گو
هم‌ساخت‌شناسی
	4193
	17246
	ENSG00000135679
	ENSMUSG00000020184
	Q00987
	P23804
	NM_001145337، NM_001145339، NM_001145340، NM_001278462، NM_002392، NM_006878، NM_006879، NM_006880، NM_006881، NM_006882، NM_032739، NM_001367990، XM_047428853 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، XM_047428853
	NM_010786، XM_017313822، XM_036155661 NM_001288586، NM_010786، XM_017313822، XM_036155661
	NP_001138811، NP_001138812، NP_001265391، NP_002383، XP_006719462، XP_006719463، NP_001354919 NP_001138809، NP_001138811، NP_001138812، NP_001265391، NP_002383، XP_006719462، XP_006719463، NP_001354919
	NP_034916، XP_017169311، XP_036011554 NP_001275515، NP_034916، XP_017169311، XP_036011554
	ویکی‌داده
مشاهده/ویرایش انسان	مشاهده/ویرایش موش

هومولوگ شمارهٔ ۲ کروموزوم دو جزئی موش (انگلیسی: Mouse double minute 2 homolog) یک پروتئین است که در انسان توسط ژن «MDM2» کُدگذاری می‌شود.^[۴]^[۵] این پروتئین یک تنظیم‌کنندهٔ منفی پروتئین سرکوبگر تومور پی۵۳ است. MDM2 همچون یوبیکویتین لیگاز ئی۳ عمل می‌کند که کارش شناسایی ترافعال‌شدگی دومِـین پایانه-N است و علاوه بر این، یک بازدارندهٔ فعال شدن رونویسی ژن پی۵۳ است.

اثر میتوژنیک MDM2 برای فرایند بهبود زخم و ترمیم بافت آسیب‌دیده ضروری است. علاوه برای اینهاُ این پروتئین یک اثر شبه فاکتور رونویسی بر روی پروتئین ان‌اف-کاپا بی دارد که مستقل از پی۵۳ است. در نتیجه MDM2 فرایند التهاب را تشدید می‌کند و هرگونه مهار این پروتئین خاصیت قوی ضدالتهابی دارد؛ بنابراین اگر بتوان جلوی عملکرد MDM2 را گرفت، می‌توان یک اثر درمانی کمکی در مدیریت سرطان و اختلالات خودایمنی لنفوپرولیفراتیو همچون لوپوس منتشر و گلومرولونفریت سریع پیشرونده ایجاد کرد.^[۶]

یکی از روش‌های مولکولی غیرفعال کردن MDM2، فسفریلاسیون آن است که اینکار به تقویت پی۵۳ منجر می‌شود. نمونه‌ای از مهارکننده‌های تعامل پروتئین‌های MDM2-p53 عبارت است از نوتلین که یک آنالوگ سیس-ایمیدازولین است.^[۷]

پروتئین MDM2 با مولکول‌های زیر تعامل پروتئین-پروتئین دارد:

ABL1^[۸]
CTBP1^[۹]
DHFR^[۱۰]
HDAC1^[۱۱]
HIF1A^[۱۲]^[۱۳]
KAT5^[۱۴]
IGF1R^[۱۵]
P16^[۱۶]^[۱۷]^[۱۸]^[۱۹]^[۲۰]
P53^[۲۱]^[۲۲]
PML^[۲۳]^[۲۴]^[۲۵]^[۲۶]
RYBP^[۲۷]

منابع

↑ ^۱٫۰ ^۱٫۱ ^۱٫۲ GRCm38: Ensembl release 89: ENSMUSG00000020184 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Oliner JD, Kinzler KW, Meltzer PS, George DL, Vogelstein B (July 1992). "Amplification of a gene encoding a p53-associated protein in human sarcomas". Nature. 358 (6381): 80–3. Bibcode:1992Natur.358...80O. doi:10.1038/358080a0. hdl:2027.42/62637. PMID 1614537. S2CID 1056405.
↑ Wade M, Wong ET, Tang M, Stommel JM, Wahl GM (November 2006). "Hdmx modulates the outcome of p53 activation in human tumor cells". The Journal of Biological Chemistry. 281 (44): 33036–44. doi:10.1074/jbc.M605405200. PMID 16905769. S2CID 16619596.
↑ Ebrahim M, Mulay SR, Anders HJ, Thomasova D (November 2015). "MDM2 beyond cancer: podoptosis, development, inflammation, and tissue regeneration". Histology and Histopathology. 30 (11): 1271–82. doi:10.14670/HH-11-636. PMID 26062755.
↑ Vassilev LT, Vu BT, Graves B, Carvajal D, Podlaski F, Filipovic Z, Kong N, Kammlott U, Lukacs C, Klein C, Fotouhi N, Liu EA (February 2004). "In vivo activation of the p53 pathway by small-molecule antagonists of MDM2". Science. 303 (5659): 844–8. Bibcode:2004Sci...303..844V. doi:10.1126/science.1092472. PMID 14704432. S2CID 16132757.
↑ Goldberg Z, Vogt Sionov R, Berger M, Zwang Y, Perets R, Van Etten RA, Oren M, Taya Y, Haupt Y (July 2002). "Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation". The EMBO Journal. 21 (14): 3715–27. doi:10.1093/emboj/cdf384. PMC 125401. PMID 12110584.
↑ Mirnezami AH, Campbell SJ, Darley M, Primrose JN, Johnson PW, Blaydes JP (July 2003). "Hdm2 recruits a hypoxia-sensitive corepressor to negatively regulate p53-dependent transcription" (PDF). Current Biology. 13 (14): 1234–9. doi:10.1016/S0960-9822(03)00454-8. PMID 12867035. S2CID 2451241.
↑ Maguire M, Nield PC, Devling T, Jenkins RE, Park BK, Polański R, Vlatković N, Boyd MT (May 2008). "MDM2 regulates dihydrofolate reductase activity through monoubiquitination". Cancer Research. 68 (9): 3232–42. doi:10.1158/0008-5472.CAN-07-5271. PMC 3536468. PMID 18451149.
↑ Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, Yao TP (November 2002). "MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation". The EMBO Journal. 21 (22): 6236–45. doi:10.1093/emboj/cdf616. PMC 137207. PMID 12426395.
↑ Chen D, Li M, Luo J, Gu W (April 2003). "Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function". The Journal of Biological Chemistry. 278 (16): 13595–8. doi:10.1074/jbc.C200694200. PMID 12606552. S2CID 85351036.
↑ Ravi R, Mookerjee B, Bhujwalla ZM, Sutter CH, Artemov D, Zeng Q, Dillehay LE, Madan A, Semenza GL, Bedi A (January 2000). "Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1alpha". Genes & Development. 14 (1): 34–44. doi:10.1101/gad.14.1.34. PMC 316350. PMID 10640274.
↑ Legube G, Linares LK, Lemercier C, Scheffner M, Khochbin S, Trouche D (April 2002). "Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation". The EMBO Journal. 21 (7): 1704–12. doi:10.1093/emboj/21.7.1704. PMC 125958. PMID 11927554.
↑ 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.
↑ 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. S2CID 13168647.
↑ Zhang Y, Wolf GW, Bhat K, Jin A, Allio T, Burkhart WA, Xiong Y (December 2003). "Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway". Molecular and Cellular Biology. 23 (23): 8902–12. doi:10.1128/MCB.23.23.8902-8912.2003. PMC 262682. PMID 14612427.
↑ Zhang Y, Xiong Y, Yarbrough WG (March 1998). "ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways". Cell. 92 (6): 725–34. doi:10.1016/S0092-8674(00)81401-4. PMID 9529249. S2CID 334187.
↑ Clark PA, Llanos S, Peters G (July 2002). "Multiple interacting domains contribute to p14ARF mediated inhibition of MDM2". Oncogene. 21 (29): 4498–507. doi:10.1038/sj.onc.1205558. PMID 12085228. S2CID 5636220.
↑ Pomerantz J, Schreiber-Agus N, Liégeois NJ, Silverman A, Alland L, Chin L, Potes J, Chen K, Orlow I, Lee HW, Cordon-Cardo C, DePinho RA (March 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. S2CID 17190271.
↑ Haupt Y, Maya R, Kazaz A, Oren M (May 1997). "Mdm2 promotes the rapid degradation of p53". Nature. 387 (6630): 296–9. Bibcode:1997Natur.387..296H. doi:10.1038/387296a0. PMID 9153395. S2CID 4336620.
↑ Honda R, Tanaka H, Yasuda H (December 1997). "Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53". FEBS Letters. 420 (1): 25–7. doi:10.1016/S0014-5793(97)01480-4. PMID 9450543. S2CID 29014813.
↑ Bernardi R, Scaglioni PP, Bergmann S, Horn HF, Vousden KH, Pandolfi PP (July 2004). "PML regulates p53 stability by sequestering Mdm2 to the nucleolus". Nature Cell Biology. 6 (7): 665–72. doi:10.1038/ncb1147. PMID 15195100. S2CID 26281860.
↑ Zhu H, Wu L, Maki CG (December 2003). "MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53". The Journal of Biological Chemistry. 278 (49): 49286–92. doi:10.1074/jbc.M308302200. PMID 14507915. S2CID 21775225.
↑ Kurki S, Latonen L, Laiho M (October 2003). "Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization". Journal of Cell Science. 116 (Pt 19): 3917–25. doi:10.1242/jcs.00714. PMID 12915590. S2CID 10448090.
↑ Wei X, Yu ZK, Ramalingam A, Grossman SR, Yu JH, Bloch DB, Maki CG (August 2003). "Physical and functional interactions between PML and MDM2". The Journal of Biological Chemistry. 278 (31): 29288–97. doi:10.1074/jbc.M212215200. PMID 12759344. S2CID 27707203.
↑ Chen D, Zhang J, Li M, Rayburn ER, Wang H, Zhang R (February 2009). "RYBP stabilizes p53 by modulating MDM2". EMBO Reports. 10 (2): 166–72. doi:10.1038/embor.2008.231. PMC 2637313. PMID 19098711.

برای مطالعهٔ بیشتر

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این یک مقالهٔ خرد زیست‌شناسی مولکولی است. می‌توانید با گسترش آن به ویکی‌پدیا کمک کنید.

[refGRCm38Ensembl-1] ۱٫۰ ^۱٫۱ ^۱٫۲ GRCm38: Ensembl release 89: ENSMUSG00000020184 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid_1614537-4] Oliner JD, Kinzler KW, Meltzer PS, George DL, Vogelstein B (July 1992). "Amplification of a gene encoding a p53-associated protein in human sarcomas". Nature. 358 (6381): 80–3. Bibcode:1992Natur.358...80O. doi:10.1038/358080a0. hdl:2027.42/62637. PMID 1614537. S2CID 1056405.

[pmid_16905769-5] Wade M, Wong ET, Tang M, Stommel JM, Wahl GM (November 2006). "Hdmx modulates the outcome of p53 activation in human tumor cells". The Journal of Biological Chemistry. 281 (44): 33036–44. doi:10.1074/jbc.M605405200. PMID 16905769. S2CID 16619596.

[6] Ebrahim M, Mulay SR, Anders HJ, Thomasova D (November 2015). "MDM2 beyond cancer: podoptosis, development, inflammation, and tissue regeneration". Histology and Histopathology. 30 (11): 1271–82. doi:10.14670/HH-11-636. PMID 26062755.

[Nutlin-7] Vassilev LT, Vu BT, Graves B, Carvajal D, Podlaski F, Filipovic Z, Kong N, Kammlott U, Lukacs C, Klein C, Fotouhi N, Liu EA (February 2004). "In vivo activation of the p53 pathway by small-molecule antagonists of MDM2". Science. 303 (5659): 844–8. Bibcode:2004Sci...303..844V. doi:10.1126/science.1092472. PMID 14704432. S2CID 16132757.

[pmid_12110584-8] Goldberg Z, Vogt Sionov R, Berger M, Zwang Y, Perets R, Van Etten RA, Oren M, Taya Y, Haupt Y (July 2002). "Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation". The EMBO Journal. 21 (14): 3715–27. doi:10.1093/emboj/cdf384. PMC 125401. PMID 12110584.

[pmid_12867035-9] Mirnezami AH, Campbell SJ, Darley M, Primrose JN, Johnson PW, Blaydes JP (July 2003). "Hdm2 recruits a hypoxia-sensitive corepressor to negatively regulate p53-dependent transcription" (PDF). Current Biology. 13 (14): 1234–9. doi:10.1016/S0960-9822(03)00454-8. PMID 12867035. S2CID 2451241.

[pmid_18451149-10] Maguire M, Nield PC, Devling T, Jenkins RE, Park BK, Polański R, Vlatković N, Boyd MT (May 2008). "MDM2 regulates dihydrofolate reductase activity through monoubiquitination". Cancer Research. 68 (9): 3232–42. doi:10.1158/0008-5472.CAN-07-5271. PMC 3536468. PMID 18451149.

[pmid_12426395-11] Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, Yao TP (November 2002). "MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation". The EMBO Journal. 21 (22): 6236–45. doi:10.1093/emboj/cdf616. PMC 137207. PMID 12426395.

[pmid_12606552-12] Chen D, Li M, Luo J, Gu W (April 2003). "Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function". The Journal of Biological Chemistry. 278 (16): 13595–8. doi:10.1074/jbc.C200694200. PMID 12606552. S2CID 85351036.

[pmid_10640274-13] Ravi R, Mookerjee B, Bhujwalla ZM, Sutter CH, Artemov D, Zeng Q, Dillehay LE, Madan A, Semenza GL, Bedi A (January 2000). "Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1alpha". Genes & Development. 14 (1): 34–44. doi:10.1101/gad.14.1.34. PMC 316350. PMID 10640274.

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