- PELP-1
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proline, glutamic acid and leucine rich protein 1 Identifiers Symbol PELP1 Entrez 27043 HUGO 30134 OMIM 609455 RefSeq NM_014389 UniProt Q8IZL8 Other data Locus Chr. 17 p13.2 PELP-1 (MNAR)[1] is a transcriptional corepressor for nuclear receptors such as glucocorticoid receptors[2] and a coactivator for estrogen receptors.[3]
Contents
Activation of protein kinases
PELP-1 has been shown to bind to both estrogen receptor alpha and estrogen receptor beta.[3] It was also reported that protein tyrosine kinases of the src family can form a complex with estrogen receptors and PELP-1 and it was reported that when bound to PELP-1 and estrogen receptor alpha the kinase activity of SRC was activated in an estrogen-sensitive manner. Mitogen-activated protein kinases ERK1 and ERK2 were found to become phosphorylated in estrogen-treated cells containing PELP-1 . It was reported that the enhancement of estrogen-induced gene transcription due to PELP-1 could be blocked by protein kinase inhibitors. This suggested a model of PELP-1 function in which estrogen and PELP-1 cooperate to activate protein kinases which in turn activate gene transcription.
Histone deacetylase
When functioning as a corepressor of transcription PELP-1 recruits histone deacetylase.[2] Estrogen has been associated with stimulation of cell proliferation and progression of cells through G1 to the S phase of the cell cycle. The retinoblastoma protein (Rb) is a regulator of G1. It was reported that PELP-1 interacts with Rb.[4] It is not known if estrogen receptors can displace histone deacetylase from Rb.
See also
External links
References
- ^ Vadlamudi RK, Kumar R (2007). "Functional and biological properties of the nuclear receptor coregulator PELP1/MNAR". Nuclear receptor signaling 5: e004. doi:10.1621/nrs.05004. PMC 1876599. PMID 17525794. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1876599.
- ^ a b Choi YB, Ko JK, Shin J (December 2004). "The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains". J. Biol. Chem. 279 (49): 50930–41. doi:10.1074/jbc.M406831200. PMID 15456770. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=15456770.
- ^ a b Vadlamudi RK, Wang RA, Mazumdar A, et al. (October 2001). "Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha". J. Biol. Chem. 276 (41): 38272–9. doi:10.1074/jbc.M103783200. PMID 11481323. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=11481323.
- ^ Balasenthil S, Vadlamudi RK (June 2003). "Functional interactions between the estrogen receptor coactivator PELP1/MNAR and retinoblastoma protein". J. Biol. Chem. 278 (24): 22119–27. doi:10.1074/jbc.M212822200. PMC 1262660. PMID 12682072. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=12682072.
Transcription coregulators Coactivators Corepressors ATP-dependent remodeling factors see also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)Categories:- Genes on chromosome 17
- Gene expression
- Transcription coregulators
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