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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
2004-6-30
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pubmed:abstractText |
The 14-3-3 proteins are known to interact with a number of proteins involved in the regulation of cell signaling. Here, we describe an association of 14-3-3zeta with the epidermal growth factor receptor (EGFR) that is rapidly induced by EGF. The 1028-EGFR truncated mutant which lacks the cytoplasmic tail from amino acids 1029-1186 identified the binding site for 14-3-3 to be between amino acid 1028 and the receptor carboxyl terminus. Mutational deletion of serine residues 1046, 1047, 1057 and 1142 did not inhibit EGF-induced 14-3-3 association with the receptor. Immunofluorescence microscopy indicated an EGF-induced co-localization of EGFR and HA-14-3-3zeta along the plasma membrane. Our finding adds to the growing complexity of EGF receptor signaling and indicates a role for 14-3-3 proteins in EGF receptor signaling or regulation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
569
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
207-10
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15225635-14-3-3 Proteins,
pubmed-meshheading:15225635-3T3 Cells,
pubmed-meshheading:15225635-Amino Acid Sequence,
pubmed-meshheading:15225635-Animals,
pubmed-meshheading:15225635-Binding Sites,
pubmed-meshheading:15225635-Conserved Sequence,
pubmed-meshheading:15225635-Epidermal Growth Factor,
pubmed-meshheading:15225635-HeLa Cells,
pubmed-meshheading:15225635-Humans,
pubmed-meshheading:15225635-Kinetics,
pubmed-meshheading:15225635-Mice,
pubmed-meshheading:15225635-Molecular Sequence Data,
pubmed-meshheading:15225635-Mutagenesis, Site-Directed,
pubmed-meshheading:15225635-Phospholipases A,
pubmed-meshheading:15225635-Receptor, Epidermal Growth Factor,
pubmed-meshheading:15225635-Recombinant Proteins,
pubmed-meshheading:15225635-Transfection,
pubmed-meshheading:15225635-Tyrosine 3-Monooxygenase
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pubmed:year |
2004
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pubmed:articleTitle |
Identification of 14-3-3zeta as an EGF receptor interacting protein.
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pubmed:affiliation |
Institute of Pathology, Rikshospitalet University Hospital, University of Oslo, N-0027 Oslo, Norway. m.p.oksvold@labmed.uio.no
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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