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Gene Review:

ATF7 - activating transcription factor 7

Homo sapiens

Synonyms: ATFA, Activating transcription factor 7, Cyclic AMP-dependent transcription factor ATF-7, Transcription factor ATF-A, cAMP-dependent transcription factor ATF-7

Hamard, P.J. et al., Peters, C.S. et al., Hamard, P.J. et al., Pescini, R. et al., Davidson, I. et al., et al.

Davidson, Kobi, Fadloun, Mengus,

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High impact information on ATF7

We have identified a novel basic leucine zipper (bZIP) protein, designated ATF-7, that physically interacts with the PRL-1 protein-tyrosine phosphatase (PTPase) [1].
ATF-7 is expressed in a number of different tissues and is expressed in association with differentiation in the Caco-2 cell model of intestinal differentiation [1].
We have isolated a cDNA encoding a variant of the transcription factor ATF-a (called ATF-a0) by screening a HeLa cDNA expression library with a regulatory element of the E-selectin promoter, NF-ELAM1/delta A [2].
A functional interaction between ATF7 and TAF12 that is modulated by TAF4 [3].
In support of this conclusion, chromatin immunoprecipitation experiments confirm the interaction of ATF7 with TAF12 on an ATF7-responsive promoter, in the absence of any artificial overexpression of both proteins [3].

Biological context of ATF7

Although both TAF12 isoforms (TAF12-1 and -2, formerly TAF(II)20 and TAF(II)15) interact with the ATF7 activation region through their histone-fold domain, only the largest, hsTAF12-1, mediates transcriptional activation through its N-terminal region [3].

Associations of ATF7 with chemical compounds

TAF4 is however essential in the retinoic acid and cAMP signalling pathways acting as a cofactor for CREB and the retinoic acid receptor, but is a negative regulator of the ATF7 transcription factor [4].

Physical interactions of ATF7

By contrast, calreticulin had no effect on specific DNA binding by the transcription factor ATF-a delta which lacks a KVFFKR-like motif in its DNA binding domain [5].

Regulatory relationships of ATF7

Furthermore, SUMO conjugation inhibits ATF7 transactivation activity by (i) impairing its association with TAF12 and (ii) blocking its binding-to-specific sequences within target promoters [6].

Other interactions of ATF7

In the present study, we investigate the functional relationships of ATF7 with hsTAF12 (formerly hsTAF(II)20/15), which has originally been identified as a component of the general transcription factor TFIID [3].
In the present article, we demonstrate that ATF7 is sumoylated in vitro (using RanBP2 as a E3-specific ligase) and in vivo [6].

References

ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase. Peters, C.S., Liang, X., Li, S., Kannan, S., Peng, Y., Taub, R., Diamond, R.H. J. Biol. Chem. (2001) [Pubmed]
ATF-a0, a novel variant of the ATF/CREB transcription factor family, forms a dominant transcription inhibitor in ATF-a heterodimers. Pescini, R., Kaszubska, W., Whelan, J., DeLamarter, J.F., Hooft van Huijsduijnen, R. J. Biol. Chem. (1994) [Pubmed]
A functional interaction between ATF7 and TAF12 that is modulated by TAF4. Hamard, P.J., Dalbies-Tran, R., Hauss, C., Davidson, I., Kedinger, C., Chatton, B. Oncogene (2005) [Pubmed]
New insights into TAFs as regulators of cell cycle and signaling pathways. Davidson, I., Kobi, D., Fadloun, A., Mengus, G. Cell Cycle (2005) [Pubmed]
Calreticulin inhibits vitamin D3 signal transduction. Wheeler, D.G., Horsford, J., Michalak, M., White, J.H., Hendy, G.N. Nucleic Acids Res. (1995) [Pubmed]
Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity. Hamard, P.J., Boyer-Guittaut, M., Camuzeaux, B., Dujardin, D., Hauss, C., Oelgeschläger, T., Vigneron, M., Kedinger, C., Chatton, B. Nucleic Acids Res. (2007) [Pubmed]

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ATF7	Bos taurus
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atf7a	Danio rerio
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atf7	Xenopus (Silurana) tropicalis

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