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Tripartite motif protein 23 (TRIM23) regulates degradation of epidermal growth factor receptor (EGFR)
Author(s) -
LE KANG,
Pacheco-Rodriguez Gustavo,
Moss Joel,
Vaughan Martha
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.548.2
Subject(s) - immunoprecipitation , epidermal growth factor receptor , ubiquitin ligase , hela , ubiquitin , microbiology and biotechnology , chemistry , biology , receptor , cancer research , cell , biochemistry , gene
Tripartite motif protein 23 (TRIM23), also known as ADP‐ribosylation factor‐domain protein (ARD) 1, is a multi‐domain 64‐kDa protein that contains ADP‐ribosylation factor, GTPase‐activating protein, and E3 ubiquitin ligase sequences. That EGFR levels were higher in ARD1−/− than in wild type MEFs was known, but the mechanism responsible remained unknown. To explore that question, we used co‐immunoprecipitation (co‐IP) to evaluate possible interactions of ARD1 and EGFR. Endogenous ARD1 and EGFR in HeLa cells were each immunoprecipitated by antibodies against the other, as was cytohesin‐1, the only known activator of the ARD1 ARF domain. Overexpression of ARD1, intended to enhance the interaction between ARD1 and EGFR, decreased the total cell EGFR. We then found that EGFR levels were increased after ARD1 depletion in HeLa cells. It appears that the interaction of ARD1 and EGFR can be important in regulation of EGFR degradation, and thereby the EGFR content of HeLa cells as well as MEFs.