Open AccessInsider Influence on ErbB Activity
Author(s) -
BenZion Shilo
Publication year - 2010
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2010.09.042
Subject(s) - biology , erbb , cytoplasm , tyrosine kinase , microbiology and biotechnology , receptor tyrosine kinase , kinase , receptor , signal transduction , ligand (biochemistry) , cancer research , biochemistry
The receptor tyrosine kinase ErbB is activated by ligand-induced dimerization, leading to transphosphorylation of the cytoplasmic kinase domains. Bill et al. (2010) now demonstrate that transphosphorylation can be modulated from within the cell by the cytoplasmic protein cytohesin, providing new insights into ErbB-dependent processes during normal development and cancer.
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