Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 42, Issue -, Pages 114-119Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST20130236
Keywords
cortical actin; dimenzation; epidermal growth factor receptor (EGFR); oligomenzation; single-molecule localization
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Funding
- Biotechnology and Biological Sciences Research Council [BB/G006911/1]
- BBSRC [BB/G007160/1, BB/G006911/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G006911/1, BB/G007160/1] Funding Source: researchfish
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Dimerization and higher-order oligomerization are believed to play an important role in the activation of the EGFR (epidermal growth factor receptor). Understanding of the process has been limited by the lack of availability of suitable methods for the measurement in cells of distances in the range 10-100 nm, too short for imaging methods and too long for spectroscopic methods such as FRET. In the present article, we review the current state of our knowledge of EGFR oligomerization, and describe results from a new single-molecule localization method that has allowed the quantitative characterization of the distribution of EGFR-EGFR distances in cells. Recent data suggest the involvement of cortical actin in regulating the formation of EGFR complexes.
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