Localizing the EGF receptor
نویسندگان
چکیده
منابع مشابه
Pinning down the EGF receptor.
According to leading investigators in the field of cellular signal transduction, the epidermal growth factor (EGF) receptor (EGFR, ErbB1, HER1), ubiquitously encountered in signaling mechanisms and thus in human tumors, is the best studied yet least prototypic of receptor tyrosine kinases in general (1). This perception arises primarily from the fact that activation of the EGFR is thought to be...
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The ErbB family of receptors, which includes the epidermal growth factor receptor (EGFR), ErbB2, ErbB3, and ErbB4, mediate signaling by EGF-like polypeptides. To better understand the role of the EGFR tyrosine kinase, we analyzed signaling by a kinase-inactive EGFR (K721M) in ErbB-devoid 32D cells. K721M alone exhibited no detectable signaling capacity, whereas coexpression of K721M with ErbB2,...
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Activation of the Drosophila EGF receptor requires the transmembrane TGF-alpha-like ligand Spitz. Recent studies have shed new light on the role of two transmembrane proteins, Star and Rhomboid, in the presentation and subsequent proteolytic processing of Spitz.
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Differing spatial scales of signaling cascades are critical for cell orientation during chemotactic responses. We used biotin EGF bound to streptavidin-coupled magnetic beads to locally stimulate cells overexpressing the EGF receptor. We have found that EGF-induced actin polymerization remains localized even under conditions of receptor overexpression. Conversely, EGF-induced ERK activation spr...
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Scatchard analyses of the binding of EGF (epidermal growth factor) to its receptor (EGFR) yield concave up Scatchard plots, indicative of some type of heterogenity in ligand-binding affinity. This was typically interpreted as being due to the presence of two independent binding sites: one of high affinity representing ≤10% of the receptor population, and one of low affinity making up the bulk o...
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ژورنال
عنوان ژورنال: Nature Cell Biology
سال: 2002
ISSN: 1465-7392,1476-4679
DOI: 10.1038/ncb0202-e22a