Functional Interaction between the p160 Coactivator Proteins and the Transcriptional Enhancer Factor Family of Transcription Factors

Belandia, Borja; Parker, Malcolm G.

doi:10.1074/jbc.c000484200

Cited by 111 publications

(99 citation statements)

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“…This sequence conservation is sufficient for functional conservation because TEF-1 substitutes for SD in wing development (24). The gene regulatory activities of TEF-1 are governed by interactions with protein cofactors (25)(26)(27). For instance, interactions of TEF-1 with Max and serum response factor (SRF) regulate the ␣-MHC gene and normal cardiac and smooth muscle development (28,29).…”

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confidence: 99%

Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain

Anbanandam

Albarado

Nguyen

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

113

132

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Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a microarray chip-based assay, we establish that known binding sites of the full-length protein are only a subset of DNA elements recognized by TEAD. Our results provide a model for understanding the regulation of genome-wide gene expression during development by TEA͞ATTS family of transcription factors.DNA-binding protein ͉ gene regulation ͉ NMR structure ͉ development ͉ Scalloped

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confidence: 99%

Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain

Anbanandam

Albarado

Nguyen

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

113

132

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“…It has recently been shown that AIB1 binds directly to the estrogen receptor (ER) (28) and that AIB1 is rate-limiting for estrogeninduced growth of MCF-7 cells (29). However, the overall role of AIB1 for breast tumorigenesis is not clear because AIB1 potentiates not only the action of estrogen (14,16) and progesterone (16) receptors but also that of various other nuclear receptors (9,15,(17)(18)(19)(20) and transcription factors (30,31). In addition, several splice variants of SRC family members have been described, although the functions of these variants remain unknown (13).…”

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confidence: 99%

An Isoform of the Coactivator AIB1 That Increases Hormone and Growth Factor Sensitivity Is Overexpressed in Breast Cancer

Reiter

Wellstein

Riegel

2001

Journal of Biological Chemistry

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The AIB1 (amplified in breast cancer 1) protein is a coactivator that potentiates the transcriptional activity of nuclear hormone receptors, and its gene is amplified in a subset of human breast cancers. Here we report a splice variant of AIB1 mRNA that lacks the exon 3 sequence. We determined that the AIB-⌬3 mRNA encoded a 130-kDa protein that lacks the NH 2 -terminal basic helix-loop-helix and a portion of the PAS (Per-Arnt-Sim homology) dimerization domain. The 130-kDa protein was detected in MCF-7 breast cancer cells at levels that were 5-10% of the full-length protein, whereas in nontransformed mammary epithelium lines, the AIB-⌬3 protein was present at significantly lower levels compared with the full-length AIB1. Consistent with this finding, the abundance of AIB1-⌬3 mRNA was increased in human breast cancer specimens relative to that in normal breast tissue. To determine whether there were phenotypic changes associated with the overexpression of the AIB-⌬3 isoform, we performed functional reporter gene assays. These revealed that the ability of AIB1-⌬3 to promote transcription mediated by the estrogen or progesterone receptors was significantly greater than that of the full-length protein. Surprisingly, the AIB1-⌬3 isoform was also more effective than AIB1 in promoting transcription induced by epidermal growth factor. Overexpression of AIB1-⌬3 may thus play an important role in sensitizing breast tumor cells to hormone or growth factor stimulation.Ligands such as estrogen and progesterone that interact with nuclear receptors regulate gene expression predominantly at the transcriptional level. The ligand-bound receptors interact specifically with DNA and activate transcription by recruiting a preinitiation complex. Although such gene activation was originally thought to be mediated by interaction of the receptors with components of the basal transcriptional machinery (1-6), a variety of screening techniques has identified a family of receptor-interacting proteins known as nuclear receptor coactivators (7-11). A common characteristic of this superfamily of proteins is that, when overexpressed in the presence of nuclear receptors, they potentiate ligand induction of transcription (12, 13). Members of the related p160 group of coactivators, which include steroid receptor coactivator 1 (SRC-1), 1 SRC-2, and SRC-3 (also known as AIB1, ACTR, RAC3, TRAM-1, and p/CIP) (14 -20), possess several similar structural features including a receptor interaction domain, a bHLH (basic helix-loop-helix)-PAS (Per-Arnt-Sim homology) dimerization domain, and a CBP interaction domain (13). Coactivators are thought to function as bridges between nuclear receptors and either other coactivators or the basal transcriptional machinery (13). However, the discovery that coactivators possess a histone acetylase domain (15,(21)(22)(23)(24) suggests that these proteins also might serve to regulate chromatin structure.A portion of human chromosome 20q that is frequently amplified in breast cancer contains the gene for the nuclear coactiva...

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“…It is proposed that activity of TEF-1 proteins is controlled by interactions with specific cofactors with limited expression patterns. Known vertebrate TEF-1 co-factors include PARP [27], the Vgl family of proteins [25,26,43], YAP65 [24] and p160 [22]. These co-factors are broadly expressed (PARP and p160), expressed in the same tissues as TEF-1 proteins (YAP65) or restricted in their expression to one or two tissues (Vgl proteins).…”

Section: Tef-1 and Rtef-1 Interact Differentially With Taz In Vivo Anmentioning

confidence: 99%

“…Class 1: interacting proteins with co-activation function [p160 steroid hormone receptor co-activators and YAP65 (Yes-associated protein 65 kDa)]. These TEF-1 co-factors contain transactivation domains, interact with TEF-1 and activate transcription of MCATdependent promoters ( [22][23][24], and see below). Class 2: interacting proteins without co-activation function [TONDU (Vgl-1, Vestigial-like protein-1), Vgl-2 and Vgl-3].…”

Section: Introductionmentioning

confidence: 99%

The transcriptional co-activator TAZ interacts differentially with transcriptional enhancer factor-1 (TEF-1) family members

Mahoney

Hong

Yaffe

et al. 2005

Biochemical Journal

192

156

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Members of the highly related TEF-1 (transcriptional enhancer factor-1) family (also known as TEAD, for TEF-1, TEC1, ABAA domain) bind to MCAT (muscle C, A and T sites) and A/T-rich sites in promoters active in cardiac, skeletal and smooth muscle, placenta, and neural crest. TEF-1 activity is regulated by interactions with transcriptional co-factors [p160, TONDU (Vgl-1, Vestigial-like protein-1), Vgl-2 and YAP65 (Yes-associated protein 65 kDa)]. The strong transcriptional co-activator YAP65 interacts with all TEF-1 family members, and, since YAP65 is related to TAZ (transcriptional co-activator with PDZ-binding motif), we wanted to determine if TAZ also interacts with members of the TEF-1 family. In the present study, we show by GST (glutathione S-transferase) pull-down assays, by co-immunoprecipitation and by modified mammalian two-hybrid assays that TEF-1 interacts with TAZ in vitro and in vivo. Electrophoretic mobility-shift assays with purified TEF-1 and GST-TAZ fusion protein showed that TAZ interacts with TEF-1 bound to MCAT DNA. TAZ can interact with endogenous TEF-1 proteins, since exogenous TAZ activated MCAT-dependent reporter promoters. Like YAP65, TAZ interacted with all four TEF-1 family members. GST pull-down assays with increasing amounts of [ 35 S]TEF-1 and [ 35 S]RTEF-1 (related TEF-1) showed that TAZ interacts more efficiently with TEF-1 than with RTEF-1. This differential interaction also extended to the interaction of TEF-1 and RTEF-1 with TAZ in vivo, as assayed by a modified mammalian twohybrid experiment. These data show that differential association of TEF-1 proteins with transcriptional co-activators may regulate the activity of TEF-1 family members.

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Functional Interaction between the p160 Coactivator Proteins and the Transcriptional Enhancer Factor Family of Transcription Factors

Cited by 111 publications

References 50 publications

Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain

Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain

An Isoform of the Coactivator AIB1 That Increases Hormone and Growth Factor Sensitivity Is Overexpressed in Breast Cancer

The transcriptional co-activator TAZ interacts differentially with transcriptional enhancer factor-1 (TEF-1) family members

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