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Updated: Aug 12, 2026

A Functional Assay for Gap Junctional Examination; Electroporation of Adherent Cells on Indium-Tin Oxide
Published on: October 18, 2014
[EGF receptor degrades via the proteasome-dependent pathway in A-431 cells]
N D Medvedeva1, A L Evdonin, N V Tsupkina
1Institute of Cytology RAS, St. Petersburg. medved@mail.cytspb.rssi.ru
Abstract:
It is known that a lot of cell receptors degrade by ubiquitine-proteasome pathway. Here we show that degradation of the epidermal growth factor (EGF) receptor is proteasome-dependent. Treatment of A-431 cells with lactacystine, an inhibitor of proteolytic activities of 26S proteasomes, induces accumulation of the receptor in cells. Incubation of cell lysates with isolated 26S proteasomes leads to diminishing EGF receptor in these cells. Active (tyrosine phosphorylated) EGF receptor is a target of proteolysis by proteasomes.
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