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Two domains of the epidermal growth factor receptor are involved in cytoskeletal interactions.

Abstract：

:Epidermal growth factor receptor can interact directly with F-actin through an actin-binding domain. In the present study, a mutant EGFR, lacking a previously identified actin-binding domain (ABD 1), was still able to bind elements of the cytoskeleton. A second EGFR actin-binding domain (ABD 2) was identified in the region of the receptor that includes Tyr-1148 by a yeast two-hybrid assay. GST fusion proteins comprising ABD 1 or ABD 2 bound actin in vitro and competed for actin-binding with the full-length EGFR. EGFR binding to actin was also studied in intact cells using fluorescence resonance energy transfer (FRET). The localization of the EGFR/actin-binding complex changed after EGF stimulation. Fusion proteins containing mutations in ABD1 or ABD2 did not display a FRET signal. The results lead to the conclusion that the interaction between ABD1 and ABD2 and actin during EGF-induced signal transduction, and thus between EGFR and actin, are important in cell activation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Song W,Wu J,Ge G,Lin Q

doi

10.1016/j.bbrc.2008.03.138

subject

Has Abstract

pub_date

2008-06-13 00:00:00

pages

589-93

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)00620-7

journal_volume

370

pub_type

杂志文章

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