From Wikipedia, the free encyclopedia
NCOA2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases NCOA2, GRIP1, KAT13C, NCoA-2, SRC2, TIF2, bHLHe75, nuclear receptor coactivator 2
External IDs OMIM: 601993; MGI: 1276533; HomoloGene: 4768; GeneCards: NCOA2; OMA: NCOA2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001077695
NM_008678
NM_001302702

RefSeq (protein)

NP_001289631
NP_032704

Location (UCSC) Chr 8: 70.11 – 70.4 Mb Chr 1: 13.14 – 13.37 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

The nuclear receptor coactivator 2 also known as NCoA-2 is a protein that in humans is encoded by the NCOA2 gene. NCoA-2 is also frequently called glucocorticoid receptor-interacting protein 1 (GRIP1), steroid receptor coactivator-2 (SRC-2), or transcriptional mediators/intermediary factor 2 (TIF2).

Function

NCoA-2 is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity. NCOA2 is recruited to DNA promotion sites by ligand-activated nuclear receptors. NCOA2 in turn acetylates histones, which makes downstream DNA more accessible to transcription. Hence, NCOA2 assists nuclear receptors in the upregulation of DNA expression. [5] [6]

GRIP1 is a transcriptional co-activator of the glucocorticoid receptor and interferon regulatory factor 1 ( IRF1). [7]

Interactions

Nuclear receptor coactivator 2 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000140396Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005886Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Voegel JJ, Heine MJ, Zechel C, Chambon P, Gronemeyer H (1996). "TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors". EMBO J. 15 (14): 3667–75. doi: 10.1002/j.1460-2075.1996.tb00736.x. PMC  452006. PMID  8670870.
  6. ^ Hong H, Kohli K, Garabedian MJ, Stallcup MR (1997). "GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors". Mol Cell Biol. 17 (5): 2735–44. doi: 10.1128/MCB.17.5.2735. PMC  232124. PMID  9111344.
  7. ^ Bhandare R, Damera G, Banerjee A, Flammer JR, Keslacy S, Rogatsky I, Panettieri RA, Amrani Y, Tliba O (January 2010). "Glucocorticoid receptor interacting protein-1 restores glucocorticoid responsiveness in steroid-resistant airway structural cells". Am. J. Respir. Cell Mol. Biol. 42 (1): 9–15. doi: 10.1165/rcmb.2009-0239RC. PMC  2809222. PMID  19805480.
  8. ^ Song LN, Coghlan M, Gelmann EP (2004). "Antiandrogen effects of mifepristone on coactivator and corepressor interactions with the androgen receptor". Mol. Endocrinol. 18 (1): 70–85. doi: 10.1210/me.2003-0189. PMID  14593076.
  9. ^ Ishitani K, Yoshida T, Kitagawa H, Ohta H, Nozawa S, Kato S (2003). "p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor". Biochem. Biophys. Res. Commun. 306 (3): 660–5. doi: 10.1016/S0006-291X(03)01021-0. PMID  12810069.
  10. ^ Wang Q, Udayakumar TS, Vasaitis TS, Brodie AM, Fondell JD (2004). "Mechanistic relationship between androgen receptor polyglutamine tract truncation and androgen-dependent transcriptional hyperactivity in prostate cancer cells". J. Biol. Chem. 279 (17): 17319–28. doi: 10.1074/jbc.M400970200. PMID  14966121.
  11. ^ a b c He B, Wilson EM (2003). "Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs". Mol. Cell. Biol. 23 (6): 2135–50. doi: 10.1128/MCB.23.6.2135-2150.2003. PMC  149467. PMID  12612084.
  12. ^ Bai S, He B, Wilson EM (2005). "Melanoma antigen gene protein MAGE-11 regulates androgen receptor function by modulating the interdomain interaction". Mol. Cell. Biol. 25 (4): 1238–57. doi: 10.1128/MCB.25.4.1238-1257.2005. PMC  548016. PMID  15684378.
  13. ^ Beischlag TV, Wang S, Rose DW, Torchia J, Reisz-Porszasz S, Muhammad K, Nelson WE, Probst MR, Rosenfeld MG, Hankinson O (2002). "Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex". Mol. Cell. Biol. 22 (12): 4319–33. doi: 10.1128/MCB.22.12.4319-4333.2002. PMC  133867. PMID  12024042.
  14. ^ Rodriguez M, Yu X, Chen J, Songyang Z (2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. 278 (52): 52914–8. doi: 10.1074/jbc.C300407200. PMID  14578343.
  15. ^ Park JJ, Irvine RA, Buchanan G, Koh SS, Park JM, Tilley WD, Stallcup MR, Press MF, Coetzee GA (2000). "Breast cancer susceptibility gene 1 (BRCAI) is a coactivator of the androgen receptor". Cancer Res. 60 (21): 5946–9. PMID  11085509.
  16. ^ a b c d Watanabe M, Yanagisawa J, Kitagawa H, Takeyama K, Ogawa S, Arao Y, Suzawa M, Kobayashi Y, Yano T, Yoshikawa H, Masuhiro Y, Kato S (2001). "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA". EMBO J. 20 (6): 1341–52. doi: 10.1093/emboj/20.6.1341. PMC  145523. PMID  11250900. (Retracted, see doi: 10.15252/embj.201470090, PMID  25452582. If this is an intentional citation to a retracted paper, please replace {{ retracted|...}} with {{ retracted|...|intentional=yes}}.)
  17. ^ a b Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell. 113 (7): 905–17. doi: 10.1016/S0092-8674(03)00436-7. PMID  12837248. (Retracted, see doi: 10.1016/j.cell.2012.03.008, PMID  22464333,   Retraction Watch. If this is an intentional citation to a retracted paper, please replace {{ retracted|...}} with {{ retracted|...|intentional=yes}}.)
  18. ^ Wärnmark A, Treuter E, Gustafsson JA, Hubbard RE, Brzozowski AM, Pike AC (2002). "Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha". J. Biol. Chem. 277 (24): 21862–8. doi: 10.1074/jbc.M200764200. PMID  11937504.
  19. ^ Fenne IS, Hoang T, Hauglid M, Sagen JV, Lien EA, Mellgren G (2008). "Recruitment of coactivator glucocorticoid receptor interacting protein 1 to an estrogen receptor transcription complex is regulated by the 3',5'-cyclic adenosine 5'-monophosphate-dependent protein kinase". Endocrinology. 149 (9): 4336–45. doi: 10.1210/en.2008-0037. PMID  18499756.
  20. ^ Zilliacus J, Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson JA (2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140". Mol. Endocrinol. 15 (4): 501–11. doi: 10.1210/mend.15.4.0624. PMID  11266503.
  21. ^ Bledsoe RK, Montana VG, Stanley TB, Delves CJ, Apolito CJ, McKee DD, Consler TG, Parks DJ, Stewart EL, Willson TM, Lambert MH, Moore JT, Pearce KH, Xu HE (2002). "Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition". Cell. 110 (1): 93–105. doi: 10.1016/S0092-8674(02)00817-6. PMID  12151000.
  22. ^ Wyszynski M, Kim E, Dunah AW, Passafaro M, Valtschanoff JG, Serra-Pagès C, Streuli M, Weinberg RJ, Sheng M (2002). "Interaction between GRIP and liprin-alpha/SYD2 is required for AMPA receptor targeting". Neuron. 34 (1): 39–52. doi: 10.1016/S0896-6273(02)00640-2. PMID  11931740.
  23. ^ Kodera Y, Takeyama K, Murayama A, Suzawa M, Masuhiro Y, Kato S (2000). "Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators". J. Biol. Chem. 275 (43): 33201–4. doi: 10.1074/jbc.C000517200. PMID  10944516. (Retracted, see doi: 10.1074/jbc.A113.000517, PMID  24143011,   Retraction Watch. If this is an intentional citation to a retracted paper, please replace {{ retracted|...}} with {{ retracted|...|intentional=yes}}.)
  24. ^ a b Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". J. Biol. Chem. 276 (44): 40614–20. doi: 10.1074/jbc.M106263200. PMID  11514567.
  25. ^ Lee WY, Noy N (2002). "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry. 41 (8): 2500–8. doi: 10.1021/bi011764+. PMID  11851396.
  26. ^ Herdick M, Steinmeyer A, Carlberg C (2000). "Antagonistic action of a 25-carboxylic ester analogue of 1alpha, 25-dihydroxyvitamin D3 is mediated by a lack of ligand-induced vitamin D receptor interaction with coactivators". J. Biol. Chem. 275 (22): 16506–12. doi: 10.1074/jbc.M910000199. PMID  10748178.

Further reading

External links

From Wikipedia, the free encyclopedia
NCOA2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases NCOA2, GRIP1, KAT13C, NCoA-2, SRC2, TIF2, bHLHe75, nuclear receptor coactivator 2
External IDs OMIM: 601993; MGI: 1276533; HomoloGene: 4768; GeneCards: NCOA2; OMA: NCOA2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001077695
NM_008678
NM_001302702

RefSeq (protein)

NP_001289631
NP_032704

Location (UCSC) Chr 8: 70.11 – 70.4 Mb Chr 1: 13.14 – 13.37 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

The nuclear receptor coactivator 2 also known as NCoA-2 is a protein that in humans is encoded by the NCOA2 gene. NCoA-2 is also frequently called glucocorticoid receptor-interacting protein 1 (GRIP1), steroid receptor coactivator-2 (SRC-2), or transcriptional mediators/intermediary factor 2 (TIF2).

Function

NCoA-2 is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity. NCOA2 is recruited to DNA promotion sites by ligand-activated nuclear receptors. NCOA2 in turn acetylates histones, which makes downstream DNA more accessible to transcription. Hence, NCOA2 assists nuclear receptors in the upregulation of DNA expression. [5] [6]

GRIP1 is a transcriptional co-activator of the glucocorticoid receptor and interferon regulatory factor 1 ( IRF1). [7]

Interactions

Nuclear receptor coactivator 2 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000140396Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005886Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Voegel JJ, Heine MJ, Zechel C, Chambon P, Gronemeyer H (1996). "TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors". EMBO J. 15 (14): 3667–75. doi: 10.1002/j.1460-2075.1996.tb00736.x. PMC  452006. PMID  8670870.
  6. ^ Hong H, Kohli K, Garabedian MJ, Stallcup MR (1997). "GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors". Mol Cell Biol. 17 (5): 2735–44. doi: 10.1128/MCB.17.5.2735. PMC  232124. PMID  9111344.
  7. ^ Bhandare R, Damera G, Banerjee A, Flammer JR, Keslacy S, Rogatsky I, Panettieri RA, Amrani Y, Tliba O (January 2010). "Glucocorticoid receptor interacting protein-1 restores glucocorticoid responsiveness in steroid-resistant airway structural cells". Am. J. Respir. Cell Mol. Biol. 42 (1): 9–15. doi: 10.1165/rcmb.2009-0239RC. PMC  2809222. PMID  19805480.
  8. ^ Song LN, Coghlan M, Gelmann EP (2004). "Antiandrogen effects of mifepristone on coactivator and corepressor interactions with the androgen receptor". Mol. Endocrinol. 18 (1): 70–85. doi: 10.1210/me.2003-0189. PMID  14593076.
  9. ^ Ishitani K, Yoshida T, Kitagawa H, Ohta H, Nozawa S, Kato S (2003). "p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor". Biochem. Biophys. Res. Commun. 306 (3): 660–5. doi: 10.1016/S0006-291X(03)01021-0. PMID  12810069.
  10. ^ Wang Q, Udayakumar TS, Vasaitis TS, Brodie AM, Fondell JD (2004). "Mechanistic relationship between androgen receptor polyglutamine tract truncation and androgen-dependent transcriptional hyperactivity in prostate cancer cells". J. Biol. Chem. 279 (17): 17319–28. doi: 10.1074/jbc.M400970200. PMID  14966121.
  11. ^ a b c He B, Wilson EM (2003). "Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs". Mol. Cell. Biol. 23 (6): 2135–50. doi: 10.1128/MCB.23.6.2135-2150.2003. PMC  149467. PMID  12612084.
  12. ^ Bai S, He B, Wilson EM (2005). "Melanoma antigen gene protein MAGE-11 regulates androgen receptor function by modulating the interdomain interaction". Mol. Cell. Biol. 25 (4): 1238–57. doi: 10.1128/MCB.25.4.1238-1257.2005. PMC  548016. PMID  15684378.
  13. ^ Beischlag TV, Wang S, Rose DW, Torchia J, Reisz-Porszasz S, Muhammad K, Nelson WE, Probst MR, Rosenfeld MG, Hankinson O (2002). "Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex". Mol. Cell. Biol. 22 (12): 4319–33. doi: 10.1128/MCB.22.12.4319-4333.2002. PMC  133867. PMID  12024042.
  14. ^ Rodriguez M, Yu X, Chen J, Songyang Z (2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. 278 (52): 52914–8. doi: 10.1074/jbc.C300407200. PMID  14578343.
  15. ^ Park JJ, Irvine RA, Buchanan G, Koh SS, Park JM, Tilley WD, Stallcup MR, Press MF, Coetzee GA (2000). "Breast cancer susceptibility gene 1 (BRCAI) is a coactivator of the androgen receptor". Cancer Res. 60 (21): 5946–9. PMID  11085509.
  16. ^ a b c d Watanabe M, Yanagisawa J, Kitagawa H, Takeyama K, Ogawa S, Arao Y, Suzawa M, Kobayashi Y, Yano T, Yoshikawa H, Masuhiro Y, Kato S (2001). "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA". EMBO J. 20 (6): 1341–52. doi: 10.1093/emboj/20.6.1341. PMC  145523. PMID  11250900. (Retracted, see doi: 10.15252/embj.201470090, PMID  25452582. If this is an intentional citation to a retracted paper, please replace {{ retracted|...}} with {{ retracted|...|intentional=yes}}.)
  17. ^ a b Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell. 113 (7): 905–17. doi: 10.1016/S0092-8674(03)00436-7. PMID  12837248. (Retracted, see doi: 10.1016/j.cell.2012.03.008, PMID  22464333,   Retraction Watch. If this is an intentional citation to a retracted paper, please replace {{ retracted|...}} with {{ retracted|...|intentional=yes}}.)
  18. ^ Wärnmark A, Treuter E, Gustafsson JA, Hubbard RE, Brzozowski AM, Pike AC (2002). "Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha". J. Biol. Chem. 277 (24): 21862–8. doi: 10.1074/jbc.M200764200. PMID  11937504.
  19. ^ Fenne IS, Hoang T, Hauglid M, Sagen JV, Lien EA, Mellgren G (2008). "Recruitment of coactivator glucocorticoid receptor interacting protein 1 to an estrogen receptor transcription complex is regulated by the 3',5'-cyclic adenosine 5'-monophosphate-dependent protein kinase". Endocrinology. 149 (9): 4336–45. doi: 10.1210/en.2008-0037. PMID  18499756.
  20. ^ Zilliacus J, Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson JA (2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140". Mol. Endocrinol. 15 (4): 501–11. doi: 10.1210/mend.15.4.0624. PMID  11266503.
  21. ^ Bledsoe RK, Montana VG, Stanley TB, Delves CJ, Apolito CJ, McKee DD, Consler TG, Parks DJ, Stewart EL, Willson TM, Lambert MH, Moore JT, Pearce KH, Xu HE (2002). "Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition". Cell. 110 (1): 93–105. doi: 10.1016/S0092-8674(02)00817-6. PMID  12151000.
  22. ^ Wyszynski M, Kim E, Dunah AW, Passafaro M, Valtschanoff JG, Serra-Pagès C, Streuli M, Weinberg RJ, Sheng M (2002). "Interaction between GRIP and liprin-alpha/SYD2 is required for AMPA receptor targeting". Neuron. 34 (1): 39–52. doi: 10.1016/S0896-6273(02)00640-2. PMID  11931740.
  23. ^ Kodera Y, Takeyama K, Murayama A, Suzawa M, Masuhiro Y, Kato S (2000). "Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators". J. Biol. Chem. 275 (43): 33201–4. doi: 10.1074/jbc.C000517200. PMID  10944516. (Retracted, see doi: 10.1074/jbc.A113.000517, PMID  24143011,   Retraction Watch. If this is an intentional citation to a retracted paper, please replace {{ retracted|...}} with {{ retracted|...|intentional=yes}}.)
  24. ^ a b Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". J. Biol. Chem. 276 (44): 40614–20. doi: 10.1074/jbc.M106263200. PMID  11514567.
  25. ^ Lee WY, Noy N (2002). "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry. 41 (8): 2500–8. doi: 10.1021/bi011764+. PMID  11851396.
  26. ^ Herdick M, Steinmeyer A, Carlberg C (2000). "Antagonistic action of a 25-carboxylic ester analogue of 1alpha, 25-dihydroxyvitamin D3 is mediated by a lack of ligand-induced vitamin D receptor interaction with coactivators". J. Biol. Chem. 275 (22): 16506–12. doi: 10.1074/jbc.M910000199. PMID  10748178.

Further reading

External links


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