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2gut

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[[Image:2gut.gif|left|200px]]
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{{STRUCTURE_2gut| PDB=2gut | SCENE= }}
{{STRUCTURE_2gut| PDB=2gut | SCENE= }}
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'''Solution structure of the trans-activation domain of the human co-activator ARC105'''
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===Solution structure of the trans-activation domain of the human co-activator ARC105===
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==Overview==
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The sterol regulatory element binding protein (SREBP) family of transcription activators are critical regulators of cholesterol and fatty acid homeostasis. We previously demonstrated that human SREBPs bind the CREB-binding protein (CBP)/p300 acetyltransferase KIX domain and recruit activator-recruited co-factor (ARC)/Mediator co-activator complexes through unknown mechanisms. Here we show that SREBPs use the evolutionarily conserved ARC105 (also called MED15) subunit to activate target genes. Structural analysis of the SREBP-binding domain in ARC105 by NMR revealed a three-helix bundle with marked similarity to the CBP/p300 KIX domain. In contrast to SREBPs, the CREB and c-Myb activators do not bind the ARC105 KIX domain, although they interact with the CBP KIX domain, revealing a surprising specificity among structurally related activator-binding domains. The Caenorhabditis elegans SREBP homologue SBP-1 promotes fatty acid homeostasis by regulating the expression of lipogenic enzymes. We found that, like SBP-1, the C. elegans ARC105 homologue MDT-15 is required for fatty acid homeostasis, and show that both SBP-1 and MDT-15 control transcription of genes governing desaturation of stearic acid to oleic acid. Notably, dietary addition of oleic acid significantly rescued various defects of nematodes targeted with RNA interference against sbp-1 and mdt-15, including impaired intestinal fat storage, infertility, decreased size and slow locomotion, suggesting that regulation of oleic acid levels represents a physiologically critical function of SBP-1 and MDT-15. Taken together, our findings demonstrate that ARC105 is a key effector of SREBP-dependent gene regulation and control of lipid homeostasis in metazoans.
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(as it appears on PubMed at http://www.pubmed.gov), where 16799563 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16799563}}
==About this Structure==
==About this Structure==
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2GUT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GUT OCA].
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2GUT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GUT OCA].
==Reference==
==Reference==
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[[Category: 3 helical bundle]]
[[Category: 3 helical bundle]]
[[Category: Kix]]
[[Category: Kix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:33:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:16:21 2008''

Revision as of 17:16, 28 July 2008

Image:2gut.png

Template:STRUCTURE 2gut

Solution structure of the trans-activation domain of the human co-activator ARC105

Template:ABSTRACT PUBMED 16799563

About this Structure

2GUT is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

An ARC/Mediator subunit required for SREBP control of cholesterol and lipid homeostasis., Yang F, Vought BW, Satterlee JS, Walker AK, Jim Sun ZY, Watts JL, DeBeaumont R, Saito RM, Hyberts SG, Yang S, Macol C, Iyer L, Tjian R, van den Heuvel S, Hart AC, Wagner G, Naar AM, Nature. 2006 Aug 10;442(7103):700-4. Epub 2006 Jun 21. PMID:16799563

Page seeded by OCA on Mon Jul 28 20:16:21 2008

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