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- W1489586498 abstract "Epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase that regulates cellular homeostatic processes. Following ligand binding, EGFR activates different downstream signalling cascades that promote cell survival, proliferation, motility, and angiogenesis and induces F-actin-dependent EGFR endocytosis, which relocalises the activated receptors for degradation or recycling. The responses that are induced by ligand binding to EGFR, including cell signalling activation, protein kinase phosphorylation and cytoskeletal network rearrangement, resemble those induced by virus infection. Increasing evidence demonstrates that many viruses usurp EGFR endocytosis or EGFR-mediated signalling for entry, replication, inflammation, and viral antagonism to the host antiviral system. In addition, viruses have acquired sophisticated mechanisms to regulate EGFR functions by interrupting the EGFR-recycling process and modulating EGFR expression. In this review, we provide an overview of the mechanisms by which viruses alter EGFR signalling in favour of their continued survival. Copyright © 2014 John Wiley & Sons, Ltd." @default.
- W1489586498 created "2016-06-24" @default.
- W1489586498 creator A5010921217 @default.
- W1489586498 creator A5041593217 @default.
- W1489586498 creator A5066962081 @default.
- W1489586498 date "2014-05-29" @default.
- W1489586498 modified "2023-09-27" @default.
- W1489586498 title "Viruses exploit the function of epidermal growth factor receptor" @default.
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