Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2003-9-29
pubmed:abstractText
Ectodomain cleavage of the ErbB-4 receptor tyrosine kinase generates a membrane-associated fragment of 80 kDa (m80) that has been subjected to N-terminal sequencing. The sequence obtained shows that the N terminus of this fragment begins with Ser-652 of ErbB-4. When a 12-residue peptide corresponding to ErbB-4 residues 646-657 was incubated with recombinant tumor necrosis factor-alpha-converting enzyme, fragments representing residues 646-651 and 652-657 were obtained. These data indicate that ectodomain cleavage of ErbB-4 occurs between His-651 and Ser-652, placing the cleavage site within the ectodomain stalk region approximately 8 residues prior to the transmembrane domain. Several experiments have characterized other aspects of the m80 ErbB-4 fragment. Inhibition of ErbB-4 tyrosine kinase activity with pan-ErbB tyrosine kinase inhibitors indicates that kinase activity is stringently required for heregulin-dependent, but not 12-O-tetradecanoylphorbol-13-acetate-induced, ErbB-4 ectodomain cleavage and formation of the m80 fragment. When the m80 ErbB-4 fragment is generated by cell treatment with heregulin or 12-O-tetradecanoylphorbol-13-acetate, the fragment associates with intact ErbB-2. However, this fragment does not associate with the intact ErbB-4 molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
38421-7
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:12869563-ADAM Proteins, pubmed-meshheading:12869563-Amino Acid Sequence, pubmed-meshheading:12869563-Animals, pubmed-meshheading:12869563-Binding Sites, pubmed-meshheading:12869563-Cell Line, pubmed-meshheading:12869563-Detergents, pubmed-meshheading:12869563-Humans, pubmed-meshheading:12869563-Metalloendopeptidases, pubmed-meshheading:12869563-Mice, pubmed-meshheading:12869563-Molecular Sequence Data, pubmed-meshheading:12869563-Peptides, pubmed-meshheading:12869563-Precipitin Tests, pubmed-meshheading:12869563-Protein Binding, pubmed-meshheading:12869563-Protein Structure, Tertiary, pubmed-meshheading:12869563-Receptor, Epidermal Growth Factor, pubmed-meshheading:12869563-Recombinant Proteins, pubmed-meshheading:12869563-Serine, pubmed-meshheading:12869563-Tetradecanoylphorbol Acetate, pubmed-meshheading:12869563-Time Factors, pubmed-meshheading:12869563-Transfection, pubmed-meshheading:12869563-Tumor Cells, Cultured
pubmed:year
2003
pubmed:articleTitle
Ectodomain cleavage of ErbB-4: characterization of the cleavage site and m80 fragment.
pubmed:affiliation
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.