NDLI: Destabilization of the epidermal growth factor receptor (EGFR) by a peptide that inhibits EGFR binding to heat shock protein 90 and receptor dimerization.

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Destabilization of the epidermal growth factor receptor (EGFR) by a peptide that inhibits EGFR binding to heat shock protein 90 and receptor dimerization.

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Destabilization of the epidermal growth factor receptor (EGFR) by a peptide that inhibits EGFR binding to heat shock protein 90 and receptor dimerization.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Osawa, Yoichi Hegde, Ashok Ramanand, Susmita G. Ray, Dipankar Whitehead, Christopher Rehemtulla, Alnawaz Morishima, Yoshihiro Pratt, William B. Lawrence, Theodore S. Ahsan, Aarif Nyati, Mukesh K.
Description	Author Affiliation: Ahsan A ( From the Departments of Radiation Oncology.)
Abstract	An eight-amino acid segment is known to be responsible for the marked difference in the rates of degradation of the EGF receptor (ErbB1) and ErbB2 upon treatment of cells with the Hsp90 inhibitor geldanamycin. We have scrambled the first six amino acids of this segment of the EGF receptor (EGFR), which lies in close association with the ATP binding cleft and the dimerization face. Scrambling these six amino acids markedly reduces EGFR stability, EGF-stimulated receptor dimerization, and autophosphorylation activity. Two peptides were synthesized as follows: one containing the wild-type sequence of the eight-amino acid segment, which we call Disruptin; and one with the scrambled sequence. Disruptin inhibits Hsp90 binding to the EGFR and causes slow degradation of the EGFR in two EGFR-dependent cancer cell lines, whereas the scrambled peptide is inactive. This effect is specific for EGFR versus other Hsp90 client proteins. In the presence of EGF, Disruptin, but not the scrambled peptide, inhibits EGFR dimerization and causes rapid degradation of the EGFR. In contrast to the Hsp90 inhibitor geldanamycin, Disruptin inhibits cancer cell growth by a nonapoptotic mechanism. Disruptin provides proof of concept for the development of a new class of anti-tumor drugs that specifically cause EGFR degradation.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	37
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-09-13
Publisher Place	United States
Access Restriction	Open
Subject Keyword	HSP90 Heat-Shock Proteins Metabolism Peptide Fragments Pharmacology Peptides Receptor, Epidermal Growth Factor Antagonists & Inhibitors Animals Antineoplastic Agents Benzoquinones CHO Cells Cell Line, Tumor Cricetulus Dimerization Drug Design Lactams, Macrocyclic Mutagenesis, Site-Directed Mutation Phosphorylation Protein Binding Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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