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A basic peptide within the juxtamembrane region is required for EGF receptor dimerization.

Abstract：

:The epidermal growth factor receptor (EGFR) is fundamental for normal cell growth and organ development, but has also been implicated in various pathologies, notably tumors of epithelial origin. We have previously shown that the initial 13 amino acids (P13) within the intracellular juxtamembrane region (R645-R657) are involved in the interaction with calmodulin, thus indicating an important role for this region in EGFR function. Here we show that P13 is required for proper dimerization of the receptor. We expressed either the intracellular domain of EGFR (TKJM) or the intracellular domain lacking P13 (DeltaTKJM) in COS-7 cells that express endogenous EGFR. Only TKJM was immunoprecipitated with an antibody directed against the extracellular part of EGFR, and only TKJM was tyrosine phosphorylated by endogenous EGFR. Using SK-N-MC cells, which do not express endogenous EGFR, that were stably transfected with either wild-type EGFR or recombinant full-length EGFR lacking P13 demonstrated that P13 is required for appropriate receptor dimerization. Furthermore, mutant EGFR lacking P13 failed to be autophosphorylated. P13 is rich in basic amino acids and in silico modeling of the EGFR in conjunction with our results suggests a novel role for the juxtamembrane domain (JM) of EGFR in mediating intracellular dimerization and thus receptor kinase activation and function.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Aifa S,Aydin J,Nordvall G,Lundström I,Svensson SP,Hermanson O

doi

10.1016/j.yexcr.2004.08.032

keywords:

subject

Has Abstract

pub_date

2005-01-01 00:00:00

pages

108-14

issue

1

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(04)00461-6

journal_volume

302

pub_type

杂志文章

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