Linked Life Data

15161351

Source:http://linkedlifedata.com/resource/pubmed/id/15161351

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-6-2
pubmed:abstractText
The mechanism of UV-radiation-induced EGF receptor (EGFR) internalization remains to be established. In the present study, we found UV-radiation-mediated internalization of the EGFR to be dependent on the cytoplasmic carboxy-terminal region. UV radiation was unable to induce internalization of EGFR carboxy-terminal truncation mutants where all or four of the five major autophosphorylation sites were missing (963- and 1028-EGFR, respectively). Mutational removal of serine residues 1046, 1047, 1057 and 1142 within the carboxy-terminal receptor region was also sufficient to abolish UV-radiation-induced internalization of the EGFR. Furthermore, the UV-radiation-induced internalization was abrogated for an EGFR mutated in tyrosine 1045 (Y1045F), the major c-Cbl binding site. However, UV radiation did not induce phosphorylation at tyrosine 1045, in contrast to the prominent phosphorylation induced by EGF. Our results suggest a mechanism for UV-radiation-induced internalization of EGFR involving a conformational change that is dependent on structural elements formed by specific serine and tyrosine residues in the carboxy-terminal domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0033-7587
pubmed:author
pubmed:issnType
Print
pubmed:volume
161
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
685-91
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15161351-Amino Acid Sequence, pubmed-meshheading:15161351-Animals, pubmed-meshheading:15161351-Cytoplasm, pubmed-meshheading:15161351-Dose-Response Relationship, Radiation, pubmed-meshheading:15161351-Mice, pubmed-meshheading:15161351-Molecular Sequence Data, pubmed-meshheading:15161351-Mutation, pubmed-meshheading:15161351-NIH 3T3 Cells, pubmed-meshheading:15161351-Platelet-Derived Growth Factor, pubmed-meshheading:15161351-Protein Conformation, pubmed-meshheading:15161351-Protein Transport, pubmed-meshheading:15161351-Receptor, Epidermal Growth Factor, pubmed-meshheading:15161351-Serine, pubmed-meshheading:15161351-Structure-Activity Relationship, pubmed-meshheading:15161351-Tissue Distribution, pubmed-meshheading:15161351-Tyrosine, pubmed-meshheading:15161351-Ultraviolet Rays
pubmed:year
2004
pubmed:articleTitle
UV-radiation-induced internalization of the epidermal growth factor receptor requires distinct serine and tyrosine residues in the cytoplasmic carboxy-terminal domain.
pubmed:affiliation
School of Surgery Pathology, University of Western Australia, Queen Elizabeth II Medical Centre, Nedlands, Western Australia 6009, Australia. m.p.oksvold@labmed.uio.no
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't