期刊
FEBS LETTERS
卷 569, 期 1-3, 页码 332-336出版社
WILEY
DOI: 10.1016/j.febslet.2004.06.014
关键词
heterodimer; epidermal growth factor; receptor; tyrosine kinase; signalling
资金
- NCI NIH HHS [R01-CA096768, R01 CA096768] Funding Source: Medline
To understand signaling by the neuregulin (NRG) receptor ErbB3/HER3, it is important to know whether ErbB3 forms homodimers upon ligand binding. Previous biophysical studies suggest that the ErbB3 extracellular region remains monomeric when bound to NRG. We used a chimeric receptor approach to address this question in living cells, fusing the extracellular region of ErbB3 to the kinase-active intracellular domain of ErbB1. The ErbB3/ErbB1 chimera responded to NRG only if ErbB2 was co-expressed in the same cells, whereas an ErbB4/ErbB1 chimera responded without ErbB2. We, therefore, suggest that ErbB3 is an obligate heterodimerization partner because of its inability to homodimerize. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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