ArticleMolecular and cellular biology2004
Functional analysis of the Mad1-mSin3A repressor-corepressor interaction reveals determinants of specificity, affinity, and transcriptional response.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed.
- Article
- Connecting the αα-hubs: same fold, disordered ligands, new functions.Cell communication and signaling : CCS · 2021Article
- An MXD1-derived repressor peptide identifies noncoding mediators of MYC-driven cell proliferation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Co-repressor, co-activator and general transcription factor: the many faces of the Sin3 histone deacetylase (HDAC) complex.The Biochemical journal · 2018Review
- Sin3A recruits Tet1 to the PAH1 domain via a highly conserved Sin3-Interaction Domain.Scientific reports · 2018Article
- Sin3a-Tet1 interaction activates gene transcription and is required for embryonic stem cell pluripotency.Nucleic acids research · 2018Article
- Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation.Scientific reports · 2016Article
- Histone deacetylase (HDAC) 1 and 2 are essential for accurate cell division and the pluripotency of embryonic stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- An overview of MYC and its interactome.Cold Spring Harbor perspectives in medicine · 2014Review
- Solution structure of the mSin3A PAH2-Pf1 SID1 complex: a Mad1/Mxd1-like interaction disrupted by MRG15 in the Rpd3S/Sin3S complex.Journal of molecular biology · 2011Article
- Adamantyl-substituted retinoid-related molecules induce apoptosis in human acute myelogenous leukemia cells.Molecular cancer therapeutics · 2010Article
- Conserved themes in target recognition by the PAH1 and PAH2 domains of the Sin3 transcriptional corepressor.Journal of molecular biology · 2008Article
- Adamantyl-substituted retinoid-related molecules bind small heterodimer partner and modulate the Sin3A repressor.Cancer research · 2007Article
- The mSin3A chromatin-modifying complex is essential for embryogenesis and T-cell development.Molecular and cellular biology · 2005Article
- Switching DNA-binding specificity by unnatural amino acid substitution.Nucleic acids research · 2005Article
- Mxi1-SRalpha: a novel Mxi1 isoform with enhanced transcriptional repression potential.Oncogene · 2004Article
- αα-Hub domains and intrinsically disordered proteins: A decisive combo.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The recruitment of corepressors by DNA-bound repressors is likely to be a critical rate-limiting step in the transcriptional regulation of many genes. An excellent paradigm for such an interaction is the association of the basic helix-loop-helix zipper protein Mad1 with the corepressor mSin3A. When bound together, the Sin3 interaction domain (SID) of Mad1 forms extensive hydrophobic contacts with the four-helix bundle formed by the paired amphipathic helix 2 (PAH2) domain of mSin3A. Using the costructure to predict the principle residues required for binding, we have carried out an extensive mutational analysis to examine the Mad1 SID-mSin3A PAH2 interaction in vitro and in vivo. Bulky hydrophobic residues in the alpha1 (I308 and V311) and alpha2 (L329 and L332) helices of the PAH2 domain are necessary to accommodate the precise arrangement of bulky (L12) and short (A15 and A16) hydrophobic residues in the amphipathic Mad1 SID. We have also used phage display to derive an optimal SID, which shows an essentially identical arrangement of key residues. By manipulating these key residues, we have generated altered-specificity Mad1 SID mutants that bind only to a PAH2 domain with a reciprocal mutation, permitting us to demonstrate for the first time that these domains interact directly in vivo. We have also found that the integrity of the PAH1 domain affects the Mad1 SID-PAH2 interaction. It is conceivable that cross talk between different PAH domains and their binding partners helps to determine the subunit composition and order of assembly of mSin3A complexes.
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