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RISS 인기검색어
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- 저자 : ( Nevan J Krogan ) (검색결과 2 건)
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CBFβ Stabilizes HIV Vif to Counteract APOBEC3 at the Expense of RUNX1 Targen Gene Expression
( Dong Young Kim ),( Eunju Kwon ),( Paul D Hartley ),( David C Crosby ),( Sumanjit Mann ),( Nevan J Krogan ),( John D Gross ) 영남대학교 약품개발연구소 2013 영남대학교 약품개발연구소 연구업적집 Vol.23 No.0
The HIV-1 accessory protein Vif hijacks a cellular Cullin-RING ubiquitin ligase, CRL5, to promote degradation of the APOBEC3 (A3) family of restriction factors. Recently, the cellular transcription cofactor CBFβ was shown to form a complex with CRL5-Vif and to be essential for A3 degradation and viral infectivity. We now demonstrate that CBFβ is required for assembling a well-ordered CRL5-Vif complex by inhibiting Vifoligomerization and by activating CRL5-Vif via direct interaction. The CRL5-Vif-CBFβ holoenzyme forms a well-defined heterohexamer, indicating that Vif simultaneously hijacks CRL5 and CBFβ. Heterodimers of CBFβ and RUNX transcription factors contribute toward the regulation of genes, including those with immune system functions. We show that binding of Vif to CBFβ is mutually exclusive with RUNX heterodimerization and impacts the expression of genes whose regulatory domains are associated with RUNX1. Our results provide a mechanism by which a pathogen with limited coding capacity uses one factor to hijack multiple host pathways.
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Yeast SREBP Cleavage Activation Requires the Golgi Dsc E3 Ligase Complex
Stewart, Emerson ,V.,Nwosu, Christine ,C.,Tong, Zongtian,Roguev, Assen,Cummins, Timothy ,D.,Kim, Dong-Uk,Hayles, Jacqueline,Park, Han-Oh,Hoe, Kwang-Lae,Powell, David ,W.,Krogan, Nevan& Elsevier 2011 Molecular cell Vol.42 No.2
<P><B>Summary</B></P><P>Mammalian lipid homeostasis requires proteolytic activation of membrane-bound sterol regulatory element binding protein (SREBP) transcription factors through sequential action of the Golgi Site-1 and Site-2 proteases. Here we report that while SREBP function is conserved in fungi, fission yeast employs a different mechanism for SREBP cleavage. Using genetics and biochemistry, we identified four genes <I>d</I>efective for <I>S</I>REBP <I>c</I>leavage, <I>dsc1-4</I>, encoding components of a transmembrane Golgi E3 ligase complex with structural homology to the Hrd1 E3 ligase complex involved in endoplasmic reticulum-associated degradation. The Dsc complex binds SREBP and cleavage requires components of the ubiquitin-proteasome pathway: the E2-conjugating enzyme Ubc4, the Dsc1 RING E3 ligase, and the proteasome. <I>dsc</I> mutants display conserved aggravating genetic interactions with components of the multivesicular body pathway in fission yeast and budding yeast, which lacks SREBP. Together, these data suggest that the Golgi Dsc E3 ligase complex functions in a post-ER pathway for protein degradation.</P> <P><B>Graphical Abstract</B></P><P><ce:figure id='dfig1'></ce:figure></P><P><B>Highlights</B></P><P>► Yeast SREBP is proteolytically activated by a different mechanism than mammalian SREBP ► Deletion collection screen identified four <I>dsc</I> genes required for fission yeast SREBP cleavage ► Dsc proteins form a Golgi E3 ligase complex that resembles Hrd1 E3 ligase in ERAD ► Yeast SREBP cleavage requires activities of the ubiquitin-proteasome pathway</P>
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