PMID- 10207062
OWN - NLM
STAT- MEDLINE
DCOM- 19990518
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 5
DP  - 1999 May
TI  - Alien, a highly conserved protein with characteristics of a corepressor for
      members of the nuclear hormone receptor superfamily.
PG  - 3383-94
AB  - Some members of nuclear hormone receptors, such as the thyroid hormone receptor
      (TR), silence gene expression in the absence of the hormone. Corepressors, which 
      bind to the receptor's silencing domain, are involved in this repression. Hormone
      binding leads to dissociation of corepressors and binding of coactivators, which 
      in turn mediate gene activation. Here, we describe the characteristics of Alien, 
      a novel corepressor. Alien interacts with TR only in the absence of hormone.
      Addition of thyroid hormone leads to dissociation of Alien from the receptor, as 
      shown by the yeast two-hybrid system, glutathione S-transferase pull-down, and
      coimmunoprecipitation experiments. Reporter assays indicate that Alien increases 
      receptor-mediated silencing and that it harbors an autonomous silencing function.
      Immune staining shows that Alien is localized in the cell nucleus. Alien is a
      highly conserved protein showing 90% identity between human and Drosophila.
      Drosophila Alien shows similar activities in that it interacts in a
      hormone-sensitive manner with TR and harbors an autonomous silencing function.
      Specific interaction of Alien is seen with Drosophila nuclear hormone receptors, 
      such as the ecdysone receptor and Seven-up, the Drosophila homologue of COUP-TF1,
      but not with retinoic acid receptor, RXR/USP, DHR 3, DHR 38, DHR 78, or DHR 96.
      These properties, taken together, show that Alien has the characteristics of a
      corepressor. Thus, Alien represents a member of a novel class of corepressors
      specific for selected members of the nuclear hormone receptor superfamily.
FAU - Dressel, U
AU  - Dressel U
AD  - Genetisches Institut der Justus-Liebig-Universitat, D-35392 Giessen, Germany.
FAU - Thormeyer, D
AU  - Thormeyer D
FAU - Altincicek, B
AU  - Altincicek B
FAU - Paululat, A
AU  - Paululat A
FAU - Eggert, M
AU  - Eggert M
FAU - Schneider, S
AU  - Schneider S
FAU - Tenbaum, S P
AU  - Tenbaum SP
FAU - Renkawitz, R
AU  - Renkawitz R
FAU - Baniahmad, A
AU  - Baniahmad A
LA  - eng
SI  - GENBANK/AF120268
SI  - GENBANK/L40388
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Alien protein, Drosophila)
RN  - 0 (COPS2 protein, human)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Insect Proteins)
RN  - 0 (Proteins)
RN  - 0 (Receptors, Glucocorticoid)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Repressor Proteins)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Transcription Factors)
RN  - EC 3.4.19.12 (COP9 Signalosome Complex)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - COP9 Signalosome Complex
MH  - Cell Line
MH  - Cell Nucleus/genetics
MH  - DNA-Binding Proteins/genetics
MH  - Drosophila
MH  - Fluorescent Antibody Technique
MH  - Genes, Reporter
MH  - Humans
MH  - Insect Proteins/chemistry/*genetics
MH  - Molecular Sequence Data
MH  - Mutation
MH  - *Proteins
MH  - Receptors, Glucocorticoid/metabolism
MH  - Receptors, Retinoic Acid/metabolism
MH  - Receptors, Thyroid Hormone/*genetics/metabolism
MH  - Repressor Proteins/*genetics
MH  - Retinoid X Receptors
MH  - Transcription Factors/metabolism
PMC - PMC84131
EDAT- 1999/04/17 00:00
MHDA- 1999/04/17 00:01
CRDT- 1999/04/17 00:00
PHST- 1999/04/17 00:00 [pubmed]
PHST- 1999/04/17 00:01 [medline]
PHST- 1999/04/17 00:00 [entrez]
AID - 10.1128/mcb.19.5.3383 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 May;19(5):3383-94. doi: 10.1128/mcb.19.5.3383.