c-Myc Interactions
Published by Anonymous on 2007/9/30 (2732 reads)
1: Curr Top Microbiol Immunol. 2006;302:123-43.
Structural aspects of interactions within the Myc/Max/Mad network.
Nair SK, Burley SK.
Department of Biochemistry and Center for Biophysics & Computational Biology, University of Illinois at Urbana-Champaign, 600 S. Mathews Avenue, Urbana, IL 61801, USA. snair@uiuc.edu
Recently determined structures of a number of Myc family proteins have provided significant insights into the molecular nature of complex assembly and DNA binding. These structures illuminate the details of specific interactions that govern the assembly of nucleoprotein complexes and, in doing so, raise more questions regarding Myc biology. In this review, we focus on the lessons provided by these structures toward understanding (1) interactions that govern transcriptional repression by Mad via the Sin3 pathway, (2) homodimerization of Max, (3) heterodimerization of Myc-Max and Mad-Max, and (4) DNA recognition by each of the Max-Max, Myc-Max, and Mad-Max dimers.
Publication Types:
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
PMID: 16620027 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Curr Top Microbiol Immunol. 1997;224:159-68.
A biochemical and biological analysis of Myc superfamily interactions.
Schreiber-Agus N, Alland L, Muhle R, Goltz J, Chen K, Stevens L, Stein D, DePinho RA.
Dept. of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, USA.
Publication Types:
Review
PMID: 9308239 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: J Investig Dermatol Symp Proc. 1996 Apr;1(2):128-35.
Functional interactions among members of the Myc superfamily and potential relevance to cutaneous growth and development.
Chin L, Liégeois N, DePinho RA, Schreiber-Agus N.
Department of Microbiology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Myc family oncoproteins function as sequence-specific transcription factors that are believed to regulate the expression of genes governing cellular growth, differentiation, and programmed cell death. Activities of Myc are countered by those of Mad and Mxi1, two related members of the Myc superfamily. Mad and Mxi1 compete with Myc for common elements and interact with putative transcriptional repressors. While the precise role of the Myc superfamily in cutaneous biology remains to be determined, findings from a number of organ systems suggest that the regulated expression and function of its members are intimately correlated with proper development and physiology. Reviewed here are current data on Myc superfamily function with references where relevant to cutaneous processes with the ultimate goal of providing a framework upon which these proteins can be exploited in gene therapeutic approaches for diseases of the skin, including neoplasia.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9627706 [PubMed - indexed for MEDLINE]
Structural aspects of interactions within the Myc/Max/Mad network.
Nair SK, Burley SK.
Department of Biochemistry and Center for Biophysics & Computational Biology, University of Illinois at Urbana-Champaign, 600 S. Mathews Avenue, Urbana, IL 61801, USA. snair@uiuc.edu
Recently determined structures of a number of Myc family proteins have provided significant insights into the molecular nature of complex assembly and DNA binding. These structures illuminate the details of specific interactions that govern the assembly of nucleoprotein complexes and, in doing so, raise more questions regarding Myc biology. In this review, we focus on the lessons provided by these structures toward understanding (1) interactions that govern transcriptional repression by Mad via the Sin3 pathway, (2) homodimerization of Max, (3) heterodimerization of Myc-Max and Mad-Max, and (4) DNA recognition by each of the Max-Max, Myc-Max, and Mad-Max dimers.
Publication Types:
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
PMID: 16620027 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Curr Top Microbiol Immunol. 1997;224:159-68.
A biochemical and biological analysis of Myc superfamily interactions.
Schreiber-Agus N, Alland L, Muhle R, Goltz J, Chen K, Stevens L, Stein D, DePinho RA.
Dept. of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, USA.
Publication Types:
Review
PMID: 9308239 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: J Investig Dermatol Symp Proc. 1996 Apr;1(2):128-35.
Functional interactions among members of the Myc superfamily and potential relevance to cutaneous growth and development.
Chin L, Liégeois N, DePinho RA, Schreiber-Agus N.
Department of Microbiology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Myc family oncoproteins function as sequence-specific transcription factors that are believed to regulate the expression of genes governing cellular growth, differentiation, and programmed cell death. Activities of Myc are countered by those of Mad and Mxi1, two related members of the Myc superfamily. Mad and Mxi1 compete with Myc for common elements and interact with putative transcriptional repressors. While the precise role of the Myc superfamily in cutaneous biology remains to be determined, findings from a number of organ systems suggest that the regulated expression and function of its members are intimately correlated with proper development and physiology. Reviewed here are current data on Myc superfamily function with references where relevant to cutaneous processes with the ultimate goal of providing a framework upon which these proteins can be exploited in gene therapeutic approaches for diseases of the skin, including neoplasia.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9627706 [PubMed - indexed for MEDLINE]
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