Source:http://linkedlifedata.com/resource/pubmed/id/12745081
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2003-5-14
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pubmed:abstractText |
The Mohr-Tranebjaerg-Jensen deafness-dystonia-optic atrophy protein DDP/TIMM8a is translated on cytoplasmic ribosomes but targeted ultimately to the mitochondrial intermembrane space, where it is involved in mitochondrial protein import. STAM1 is a cytoplasmic signal-transducing adaptor molecule implicated in cytokine signaling. We report here a direct interaction between DDP and STAM1, identified by yeast two-hybrid screening and confirmed by co-immunoprecipitation, fusion protein "pull downs," and nuclear redistribution assays. DDP coordinates Zn(2+), and Zn(2+) was found to stimulate the DDP-STAM1 interaction in vitro. Endogenous STAM1 localizes predominantly to early endosomes, and we found no evidence that STAM1 is imported into mitochondria in vitro. Thus, the DDP-STAM1 interaction likely occurs in the cytoplasm or at the mitochondrial outer membrane. The DDP-STAM1 interaction requires a coiled-coil region in STAM1 that overlaps with the immunoreceptor tyrosine-based activation motif (ITAM), a region previously shown to be important for interaction with Jak2/3 and hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs). Thus, DDP binding may alter the interactions of STAM1 with several cytoplasmic proteins involved in cell signaling and endosomal trafficking.
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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/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TIMM8A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
305
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
345-52
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12745081-Amino Acid Sequence,
pubmed-meshheading:12745081-Animals,
pubmed-meshheading:12745081-COS Cells,
pubmed-meshheading:12745081-Cell Nucleus,
pubmed-meshheading:12745081-Cytoplasm,
pubmed-meshheading:12745081-Membrane Transport Proteins,
pubmed-meshheading:12745081-Phosphoproteins,
pubmed-meshheading:12745081-Proteins,
pubmed-meshheading:12745081-Rats,
pubmed-meshheading:12745081-Rats, Sprague-Dawley,
pubmed-meshheading:12745081-Two-Hybrid System Techniques,
pubmed-meshheading:12745081-Zinc
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pubmed:year |
2003
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pubmed:articleTitle |
Interaction of the deafness-dystonia protein DDP/TIMM8a with the signal transduction adaptor molecule STAM1.
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pubmed:affiliation |
Cellular Neurology Unit, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Building 36, Room 5W21, 9000 Rockville Pike, Bethesda, MD 20892-4164, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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