Source:http://linkedlifedata.com/resource/pubmed/id/16648306
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2006-5-1
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| pubmed:databankReference | |
| pubmed:abstractText |
Activin type II receptors (ActRIIs) including ActRIIA and ActRIIB are serine/threonine kinase receptors that form complexes with type I receptors to transmit intracellular signaling of activins, nodal, myostatin and a subset of bone morphogenetic proteins. ActRIIs are unique among serine/threonine kinase receptors in that they associate with proteins having PSD-95, Discs large and ZO-1 (PDZ) domains. In our previous studies, we reported specific interactions of ActRIIs with two independent PDZ proteins named activin receptor-interacting proteins 1 and 2 (ARIP1 and ARIP2). Overexpression of both ARIP1 and ARIP2 reduce activin-induced transcription. Here, we report the isolation of two isoforms of ARIP2 named ARIP2b and 2c. ARIP2, ARIP2b and ARIP2c recognize COOH-terminal residues of ActRIIA that match a PDZ-binding consensus motif. ARIP2 and its isoforms have one PDZ domain in the NH2-terminal region, and interact with ActRIIA. Although PDZ domains containing GLGF motifs of ARIP2b and 2c are identical to that of ARIP2, their COOH-terminal sequences differ from that of ARIP2. Interestingly, unlike ARIP2, overexpression of ARIP2b or 2c did not affect ActRIIA internalization. ARIP2b/2c inhibit inhibitory actions of ARIP2 on activin signaling. ARIP2 is widely distributed in mouse tissues. ARIP2b/2c is expressed in more restricted tissues such as heart, brain, kidneys and liver. Our results indicate that although both ARIP2 and ARIP2b/2c interact with activin receptors, they regulate ActRIIA function in a different manner.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Activin Receptors, Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Activins,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Follicle Stimulating Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Reps2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Synj2bp protein, mouse
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
0022-0795
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
189
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
409-21
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:16648306-Activin Receptors, Type II,
pubmed-meshheading:16648306-Activins,
pubmed-meshheading:16648306-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:16648306-Amino Acid Sequence,
pubmed-meshheading:16648306-Animals,
pubmed-meshheading:16648306-Brain,
pubmed-meshheading:16648306-CHO Cells,
pubmed-meshheading:16648306-Calcium-Binding Proteins,
pubmed-meshheading:16648306-Cells, Cultured,
pubmed-meshheading:16648306-Cricetinae,
pubmed-meshheading:16648306-Endocytosis,
pubmed-meshheading:16648306-Follicle Stimulating Hormone,
pubmed-meshheading:16648306-Isomerism,
pubmed-meshheading:16648306-Kidney,
pubmed-meshheading:16648306-Liver,
pubmed-meshheading:16648306-Membrane Proteins,
pubmed-meshheading:16648306-Mice,
pubmed-meshheading:16648306-Molecular Sequence Data,
pubmed-meshheading:16648306-Myocardium,
pubmed-meshheading:16648306-Signal Transduction
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| pubmed:year |
2006
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| pubmed:articleTitle |
Characterization of isoforms of activin receptor-interacting protein 2 that augment activin signaling.
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| pubmed:affiliation |
The Institute for Enzyme Research, University of Tokushima, 3-18-15 Kuramoto, Tokushima 770-8503, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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