Show simple item record

COMMD1 promotes the ubiquitination of NF‐κB subunits through a cullin‐containing ubiquitin ligase

dc.contributor.authorMaine, Gabriel Nen_US
dc.contributor.authorMao, Xichengen_US
dc.contributor.authorKomarck, Christine Men_US
dc.contributor.authorBurstein, Ezraen_US
dc.date.accessioned2014-01-08T20:35:03Z
dc.date.available2014-01-08T20:35:03Z
dc.date.issued2007-01-24en_US
dc.identifier.citationMaine, Gabriel N; Mao, Xicheng; Komarck, Christine M; Burstein, Ezra (2007). "COMMD1 promotes the ubiquitination of NF‐κB subunits through a cullin‐containing ubiquitin ligase." The EMBO Journal 26(2): 436-447. <http://hdl.handle.net/2027.42/102213>en_US
dc.identifier.issn0261-4189en_US
dc.identifier.issn1460-2075en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/102213
dc.publisherJohn Wiley & Sons, Ltden_US
dc.subject.otherUbiquitinationen_US
dc.subject.otherCOMMD1en_US
dc.subject.otherCullinen_US
dc.subject.otherNF‐κBen_US
dc.subject.otherTranscriptionen_US
dc.titleCOMMD1 promotes the ubiquitination of NF‐κB subunits through a cullin‐containing ubiquitin ligaseen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.identifier.pmid17183367en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/102213/1/emboj7601489.pdf
dc.identifier.doi10.1038/sj.emboj.7601489en_US
dc.identifier.sourceThe EMBO Journalen_US
dc.identifier.citedreferenceTergaonkar V, Correa RG, Ikawa M, Verma IM ( 2005 ) Distinct roles of IκB proteins in regulating constitutive NF‐κB activity. Nat Cell Biol 7: 921 – 923en_US
dc.identifier.citedreferenceEndo TA, Masuhara M, Yokouchi M, Suzuki R, Sakamoto H, Mitsui K, Matsumoto A, Tanimura S, Ohtsubo M, Misawa H, Miyazaki T, Leonor N, Taniguchi T, Fujita T, Kanakura Y, Komiya S, Yoshimura A ( 1997 ) A new protein containing an SH2 domain that inhibits JAK kinases. Nature 387: 921 – 924en_US
dc.identifier.citedreferenceGanesh L, Burstein E, Guha‐Niyogi A, Louder MK, Mascola JR, Klomp LW, Wijmenga C, Duckett CS, Nabel GJ ( 2003 ) The gene product Murr1 restricts HIV‐1 replication in resting CD4 + lymphocytes. Nature 426: 853 – 857en_US
dc.identifier.citedreferenceHenkel T, Machleidt T, Alkalay I, Krönke M, Ben‐Neriah Y, Baeuerle PA ( 1993 ) Rapid proteolysis of IκB‐α is necessary for activation of transcription factor NF‐κB. Nature 365: 182 – 185en_US
dc.identifier.citedreferenceHoffmann A, Levchenko A, Scott ML, Baltimore D ( 2002 ) The IκB–NF‐κB signaling module: temporal control and selective gene activation. Science 298: 11241 – 11245en_US
dc.identifier.citedreferenceKarin M, Lin A ( 2002 ) NF‐κB at the crossroads of life and death. Nat Immunol 3: 221 – 227en_US
dc.identifier.citedreferenceLois C, Hong EJ, Pease S, Brown EJ, Baltimore D ( 2002 ) Germline transmission and tissue‐specific expression of transgenes delivered by lentiviral vectors. Science 295: 868 – 872en_US
dc.identifier.citedreferenceNaka T, Narazaki M, Hirata M, Matsumoto T, Minamoto S, Aono A, Nishimoto N, Kajita T, Taga T, Yoshizaki K, Akira S, Kishimoto T ( 1997 ) Structure and function of a new STAT‐induced STAT inhibitor. Nature 387: 924 – 929en_US
dc.identifier.citedreferencePause A, Lee S, Worrell RA, Chen DY, Burgess WH, Linehan WM, Klausner RD ( 1997 ) The von Hippel–Lindau tumor‐suppressor gene product forms a stable complex with human CUL‐2, a member of the Cdc53 family of proteins. Proc Natl Acad Sci USA 94: 2156 – 2161en_US
dc.identifier.citedreferenceRui L, Yuan M, Frantz D, Shoelson S, White MF ( 2002 ) SOCS‐1 and SOCS‐3 block insulin signaling by ubiquitin‐mediated degradation of IRS1 and IRS2. J Biol Chem 277: 42394 – 42398en_US
dc.identifier.citedreferenceRyo A, Suizu F, Yoshida Y, Perrem K, Liou YC, Wulf G, Rottapel R, Yamaoka S, Lu KP ( 2003 ) Regulation of NF‐κB signaling by Pin1‐dependent prolyl isomerization and ubiquitin‐mediated proteolysis of p65/RelA. Mol Cell 12: 1413 – 1426en_US
dc.identifier.citedreferenceSaccani S, Marazzi I, Beg AA, Natoli G ( 2004 ) Degradation of promoter‐bound p65/RelA is essential for the prompt termination of the nuclear factor κB response. J Exp Med 200: 107 – 113en_US
dc.identifier.citedreferenceSakurai H, Chiba H, Miyoshi H, Sugita T, Toriumi W ( 1999 ) IκB kinases phosphorylate NF‐κB p65 subunit on serine 536 in the transactivation domain. J Biol Chem 274: 30353 – 30356en_US
dc.identifier.citedreferenceUngureanu D, Saharinen P, Junttila I, Hilton DJ, Silvennoinen O ( 2002 ) Regulation of Jak2 through the ubiquitin–proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS‐1. Mol Cell Biol 22: 3316 – 3326en_US
dc.identifier.citedreferencevan de Sluis B, Rothuizen J, Pearson PL, van Oost BA, Wijmenga C ( 2002 ) Identification of a new copper metabolism gene by positional cloning in a purebred dog population. Hum Mol Genet 11: 165 – 173en_US
dc.identifier.citedreferencevon der Lehr N, Johansson S, Wu S, Bahram F, Castell A, Cetinkaya C, Hydbring P, Weidung I, Nakayama K, Nakayama KI, Soderberg O, Kerppola TK, Larsson LG ( 2003 ) The F‐box protein Skp2 participates in c‐Myc proteosomal degradation and acts as a cofactor for c‐Myc‐regulated transcription. Mol Cell 11: 1189 – 1200en_US
dc.identifier.citedreferenceVuong BQ, Arenzana TL, Showalter BM, Losman J, Chen XP, Mostecki J, Banks AS, Limnander A, Fernandez N, Rothman PB ( 2004 ) SOCS‐1 localizes to the microtubule organizing complex‐associated 20S proteasome. Mol Cell Biol 24: 9092 – 9101en_US
dc.identifier.citedreferenceWillems AR, Schwab M, Tyers M ( 2004 ) A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim Biophys Acta 1695: 133 – 170en_US
dc.identifier.citedreferenceYaron A, Hatzubai A, Davis M, Lavon I, Amit S, Manning AM, Andersen JS, Mann M, Mercurio F, Ben‐Neriah Y ( 1998 ) Identification of the receptor component of the IκBα‐ubiquitin ligase. Nature 396: 590 – 594en_US
dc.identifier.citedreferenceZhang Y, Broser M, Rom WN ( 1994 ) Activation of the interleukin 6 gene by Mycobacterium tuberculosis or lipopolysaccharide is mediated by nuclear factors NF‐IL6 and NF‐κB. Proc Natl Acad Sci USA 91: 2225 – 2229en_US
dc.identifier.citedreferenceZhong H, May MJ, Jimi E, Ghosh S ( 2002 ) The phosphorylation status of nuclear NF‐κB determines its association with CBP/p300 or HDAC‐1. Mol Cell 9: 625 – 636en_US
dc.identifier.citedreferenceBurstein E, Ganesh L, Dick RD, van De Sluis B, Wilkinson JC, Klomp LW, Wijmenga C, Brewer GJ, Nabel GJ, Duckett CS ( 2004 ) A novel role for XIAP in copper homeostasis through regulation of MURR1. EMBO J 23: 244 – 254en_US
dc.identifier.citedreferenceBurstein E, Hoberg JE, Wilkinson AS, Rumble JM, Csomos RA, Komarck CM, Maine GN, Wilkinson JC, Mayo MW, Duckett CS ( 2005 ) COMMD proteins: a novel family of structural and functional homologs of MURR1. J Biol Chem 280: 22222 – 22232en_US
dc.identifier.citedreferenceChen L, Fischle W, Verdin E, Greene WC ( 2001 ) Duration of nuclear NF‐κB action regulated by reversible acetylation. Science 293: 1653 – 1657en_US
dc.identifier.citedreferenceChen XP, Losman JA, Cowan S, Donahue E, Fay S, Vuong BQ, Nawijn MC, Capece D, Cohan VL, Rothman PB ( 2002 ) Pim serine/threonine kinases regulate the stability of Socs‐1 protein. Proc Natl Acad Sci USA 99: 2175 – 2180en_US
dc.identifier.citedreferenceChen Z, Hagler J, Palombella VJ, Melandri F, Scherer D, Ballard D, Maniatis T ( 1995 ) Signal‐induced site‐specific phosphorylation targets IκBα to the ubiquitin–proteasome pathway. Genes Dev 9: 1586 – 1597en_US
dc.identifier.citedreferenceDiamond MS, Staunton DE, Marlin SD, Springer TA ( 1991 ) Binding of the integrin Mac‐1 (CD11b/CD18) to the third immunoglobulin‐like domain of ICAM‐1 (CD54) and its regulation by glycosylation. Cell 65: 961 – 971en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.