Use of suppressor mutants to probe the function of estrogen receptor-p160 coactivator interactions

Molecular and Cellular Biology

Volumn 21, Issue 13, 2001, Pages 4379-4390

  Mak, H Y ^a   Parker, M G ^a  

^a HAMMERSMITH HOSPITAL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; ESTROGEN RECEPTOR; ESTROGEN RECEPTOR ALPHA; PROTEIN; PROTEIN COACTIVATOR; UNCLASSIFIED DRUG;

ARTICLE; CELL LEVEL; GENE TARGETING; GENETIC TRANSCRIPTION; MAMMAL CELL; MOUSE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION; REPORTER GENE; SUPPRESSOR CELL;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CARRIER PROTEINS; CELL LINE; ESTROGEN RECEPTOR ALPHA; FEMALE; GENES, REPORTER; HISTONE ACETYLTRANSFERASES; HUMANS; IMMUNOBLOTTING; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEAR PROTEINS; NUCLEOCYTOPLASMIC TRANSPORT PROTEINS; PROTEIN BINDING; RECEPTORS, ESTROGEN; RECOMBINANT FUSION PROTEINS; TRANS-ACTIVATION (GENETICS); TRANS-ACTIVATORS; TRANSCRIPTION FACTORS; TWO-HYBRID SYSTEM TECHNIQUES;

MAMMALIA;

EID: 0034975793     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.21.13.4379-4390.2001     Document Type: Article

References (48)

1. The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1
2. Molecular basis of agonism and antagonism in the oestrogen receptor
3. Functional interactions between the estrogen receptor and DRIP205, a subunit of the heteromeric DRIP coactivator complex
4. Cloning and characterization of RAP250, a novel nuclear receptor coactivator
5. Nuclear receptor coactivator ACTR is a novel historic acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
6. Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
7. Use of altered specificity mutants to probe a specific protein-protein interaction in differentiation: The GATA-1:FOG complex
8. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
9. Structure and specificity of nuclear receptor-coactivator interactions
10. Steroid and nuclear receptors
11. Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): Multiple motifs with different binding specificities
12. Thyroid hormone receptor-associated proteins and general positive cofactors mediate thyroid hormone receptor function in the absence of the TATA boxbinding protein-associated factors of TFIID
13. Increasing the complexity of coactivation in nuclear receptor signaling
14. The coregulator exchange in transcriptional functions of nuclear receptors
15. A signature motif in transcriptional co-activators mediates binding to nuclear receptors
16. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
17. Isoforms of steroid receptor coactivator 1 differ in their ability to potentiate transcription by the oestrogen receptor
18. A possible involvement of TIF1α and TIF1β in the epigenetic control of transcription by nuclear receptors
19. A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo
20. Differential mechanisms of nuclear receptor regulation by receptor-associated coactivator 3
21. Target of the transcriptional activation function of phage lambda cI protein
22. A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein
23. Molecular determinants of the estrogen receptor-coactivator interface
24. Transcriptional regulation through mediator-like coactivators in yeast and metazoan cells
25. The nuclear receptor superfamily: The second decade
26. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation
27. Nuclear receptor coregulators: Cellular and molecular biology
28. The nuclear receptor ligand-binding domain: Structure and function
29. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma
30. Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding
31. The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes
32. Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex
33. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
34. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
35. Selective use of TBP and TFIlB revealed by a TATA-TBP-TFIIB array with altered specificity
36. Modulation of estrogen receptor-alpha transcriptional activity by the coactivator PGC-1
37. The human estrogen receptor has two independent non-acidic transcriptional activation functions
38. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
39. Competition between thyroid hormone receptor-associated protein (TRAP) 220 and transcriptional intermediary factor (TIF) 2 for binding to nuclear receptors. Implications for the recruitment of TRAP and p160 coactivator complexes
40. The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways
41. Nuclear-receptor ligands and ligand-binding domains
42. UNC-4/UNC-37-dependent repression of motor neuron-specific genes controls synaptic choice in Caenorhabditis elegans
43. A canonical structure for the ligand-binding domain of nuclear receptors
44. The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/ TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development
45. Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1)
46. Discrete roles for peroxisome proliferator-activated receptor γ and retinoid X receptor in recruiting nuclear receptor coactivators
47. The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion
48. Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor