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rdf:type |
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|
lifeskim:mentions |
|
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pubmed:issue |
2
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|
pubmed:dateCreated |
1996-6-4
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|
pubmed:abstractText |
The human mineralocorticoid receptor of the steroid receptor family contains a modular structure with domain E which is considered to be a hormone binding domain. Recombinant protein approaches enabled us to clearly determine that this domain is also able to interact with F-actin (Kd about 2 microM) and G-actin. Moreover, it was revealed that this mineralocorticoid receptor domain/actin interaction was modulated by specific mineralocorticoid ligands. Agonist (aldosterone) steroid binding almost totally (91%) abolished the interaction with F-actin, while antagonist (progesterone) binding allowed more than 30% of this binding. Steroid modulation of the interaction between domain E and actin indicated that this actin binding is specific and could be essential for cellular mineralocorticoid receptor activity.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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|
pubmed:issn |
0014-5793
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
15
|
|
pubmed:volume |
384
|
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
112-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8612804-Actins,
pubmed-meshheading:8612804-Aldosterone,
pubmed-meshheading:8612804-Binding Sites,
pubmed-meshheading:8612804-Heat-Shock Proteins,
pubmed-meshheading:8612804-Humans,
pubmed-meshheading:8612804-Ligands,
pubmed-meshheading:8612804-Mineralocorticoids,
pubmed-meshheading:8612804-Peptide Fragments,
pubmed-meshheading:8612804-Progesterone,
pubmed-meshheading:8612804-Protein Binding,
pubmed-meshheading:8612804-Receptors, Mineralocorticoid,
pubmed-meshheading:8612804-Recombinant Fusion Proteins
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pubmed:year |
1996
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|
pubmed:articleTitle |
Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation.
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|
pubmed:affiliation |
Institut National de la Santé et de la Recherche Médicale, Unité 300, Faculté de Pharmacie, Montpellier, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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