The nuclear receptor co-repressor 2 (NCOR2) is a
transcriptional coregulatory protein that contains several
nuclear receptor-interacting domains. In addition, NCOR2 appears to recruit
histone deacetylases to DNA promoter regions. Hence NCOR2 assists nuclear receptors in the down
regulation of target gene expression.[5][6] NCOR2 is also referred to as a silencing mediator for retinoid or thyroid-hormone receptors (SMRT)[5] or T3 receptor-associating cofactor 1 (TRAC-1).[6]
Function
NCOR2/SMRT is a transcriptional coregulatory protein that contains several modulatory functional domains including multiple autonomous repression domains as well as two or three
C-terminal nuclear receptor-interacting domains.[5] NCOR2/SMRT serves as a repressive coregulatory factor (
corepressor) for multiple
transcription factor pathways. In this regard, NCOR2/SMRT functions as a platform protein, facilitating the recruitment of
histone deacetylases to the DNA promoters bound by its interacting transcription factors.[7]
Family
It is a member of the family of nuclear receptor corepressors; the other human protein that is a member of that family is
Nuclear receptor co-repressor 1.[8]
Discovery
SMRT was initially cloned and characterized in the laboratory of Dr.
Ronald M. Evans at the Salk Institute for Biological Studies.[5] In another early investigation into this molecule, similar findings were reported in a variant referred to as TRAC-1.[6]
Interactions
Nuclear receptor co-repressor 2 has been shown to
interact with:
^
abTagami T, Lutz WH, Kumar R, Jameson JL (December 1998). "The interaction of the vitamin D receptor with nuclear receptor corepressors and coactivators". Biochemical and Biophysical Research Communications. 253 (2): 358–63.
doi:
10.1006/bbrc.1998.9799.
PMID9878542.
^Puccetti E, Obradovic D, Beissert T, Bianchini A, Washburn B, Chiaradonna F, Boehrer S, Hoelzer D, Ottmann OG, Pelicci PG, Nervi C, Ruthardt M (December 2002). "AML-associated translocation products block vitamin D(3)-induced differentiation by sequestering the vitamin D(3) receptor". Cancer Research. 62 (23): 7050–8.
PMID12460926.
Further reading
Hörlein AJ, Näär AM, Heinzel T, Torchia J, Gloss B, Kurokawa R, Ryan A, Kamei Y, Söderström M, Glass CK (October 1995). "Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor". Nature. 377 (6548): 397–404.
Bibcode:
1995Natur.377..397H.
doi:
10.1038/377397a0.
PMID7566114.
S2CID4230850.
Margolis RL, Abraham MR, Gatchell SB, Li SH, Kidwai AS, Breschel TS, Stine OC, Callahan C, McInnis MG, Ross CA (July 1997). "cDNAs with long CAG trinucleotide repeats from human brain". Human Genetics. 100 (1): 114–22.
doi:
10.1007/s004390050476.
PMID9225980.
S2CID25999127.
Nguyen TA, Hoivik D, Lee JE, Safe S (July 1999). "Interactions of nuclear receptor coactivator/corepressor proteins with the aryl hydrocarbon receptor complex". Archives of Biochemistry and Biophysics. 367 (2): 250–7.
doi:
10.1006/abbi.1999.1282.
PMID10395741.
The nuclear receptor co-repressor 2 (NCOR2) is a
transcriptional coregulatory protein that contains several
nuclear receptor-interacting domains. In addition, NCOR2 appears to recruit
histone deacetylases to DNA promoter regions. Hence NCOR2 assists nuclear receptors in the down
regulation of target gene expression.[5][6] NCOR2 is also referred to as a silencing mediator for retinoid or thyroid-hormone receptors (SMRT)[5] or T3 receptor-associating cofactor 1 (TRAC-1).[6]
Function
NCOR2/SMRT is a transcriptional coregulatory protein that contains several modulatory functional domains including multiple autonomous repression domains as well as two or three
C-terminal nuclear receptor-interacting domains.[5] NCOR2/SMRT serves as a repressive coregulatory factor (
corepressor) for multiple
transcription factor pathways. In this regard, NCOR2/SMRT functions as a platform protein, facilitating the recruitment of
histone deacetylases to the DNA promoters bound by its interacting transcription factors.[7]
Family
It is a member of the family of nuclear receptor corepressors; the other human protein that is a member of that family is
Nuclear receptor co-repressor 1.[8]
Discovery
SMRT was initially cloned and characterized in the laboratory of Dr.
Ronald M. Evans at the Salk Institute for Biological Studies.[5] In another early investigation into this molecule, similar findings were reported in a variant referred to as TRAC-1.[6]
Interactions
Nuclear receptor co-repressor 2 has been shown to
interact with:
^
abTagami T, Lutz WH, Kumar R, Jameson JL (December 1998). "The interaction of the vitamin D receptor with nuclear receptor corepressors and coactivators". Biochemical and Biophysical Research Communications. 253 (2): 358–63.
doi:
10.1006/bbrc.1998.9799.
PMID9878542.
^Puccetti E, Obradovic D, Beissert T, Bianchini A, Washburn B, Chiaradonna F, Boehrer S, Hoelzer D, Ottmann OG, Pelicci PG, Nervi C, Ruthardt M (December 2002). "AML-associated translocation products block vitamin D(3)-induced differentiation by sequestering the vitamin D(3) receptor". Cancer Research. 62 (23): 7050–8.
PMID12460926.
Further reading
Hörlein AJ, Näär AM, Heinzel T, Torchia J, Gloss B, Kurokawa R, Ryan A, Kamei Y, Söderström M, Glass CK (October 1995). "Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor". Nature. 377 (6548): 397–404.
Bibcode:
1995Natur.377..397H.
doi:
10.1038/377397a0.
PMID7566114.
S2CID4230850.
Margolis RL, Abraham MR, Gatchell SB, Li SH, Kidwai AS, Breschel TS, Stine OC, Callahan C, McInnis MG, Ross CA (July 1997). "cDNAs with long CAG trinucleotide repeats from human brain". Human Genetics. 100 (1): 114–22.
doi:
10.1007/s004390050476.
PMID9225980.
S2CID25999127.
Nguyen TA, Hoivik D, Lee JE, Safe S (July 1999). "Interactions of nuclear receptor coactivator/corepressor proteins with the aryl hydrocarbon receptor complex". Archives of Biochemistry and Biophysics. 367 (2): 250–7.
doi:
10.1006/abbi.1999.1282.
PMID10395741.