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Endocytosed epidermal growth factor (EGF) receptors contribute to the EGF-mediated growth arrest in A431 cells by inducing a sustained increase in p21/CIP1.

Abstract：

:We investigated the ability of endocytosed activated epidermal growth factor receptors (EGFR) to induce expression of the cyclin-interacting protein p21/CIP1 in A431 cells. Transforming growth factor alpha (TGFalpha) and EGF both induced tyrosine phosphorylation, induction of p21/CIP1, and thereby inhibition of DNA synthesis. TGFalpha is released from the EGFR when the TGFalpha-EGFR complex encounters low pH upon endocytosis. Consistently, we found more rapid dephosphorylation of the EGFR and less induction of p21/CIP1 by TGFalpha than by EGF. This difference was abolished upon neutralizing endosomal pH by the carboxylic ionophore monensin or the proton ATPase inhibitor bafilomycin A1. When surface-bound TGFalpha was removed by acid stripping and endosomal pH was neutralized with bafilomycin A1, TGFalpha stimulated EGFR tyrosine phosphorylation, induced p21/CIP1, and inhibited DNA synthesis. This strongly suggests that p21/CIP1 can be induced by endocytosed, activated EGFR and that endocytosed EGFR can affect cell growth.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Skarpen E,Johannessen LE,Bjerk K,Fasteng H,Guren TK,Lindeman B,Thoresen GH,Christoffersen T,Stang E,Huitfeldt HS,Madshus IH

doi

10.1006/excr.1998.4127

subject

Has Abstract

pub_date

1998-08-25 00:00:00

pages

161-72

issue

1

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(98)94127-1

journal_volume

243

pub_type

杂志文章

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