Degradation signals in ErbB-2 dictate proteasomal processing and immunogenicity and resist protection by cis glycine-alanine repeat.

Abstract:

:ErbB-2 is ubiquitinated and degraded when dissociated from its membrane chaperone or bound by specific antibody. Reagents which induce such degradation have demonstrated antitumor activity and may impact ErbB-2 immunogenicity. To further understand ErbB-2 degradation and immunogenicity, a glycine-alanine repeat (GAr) or the reverse proline-alanine repeat (PAr) which protects certain proteins from proteasome degradation, was inserted after amino acid 5 (GAr5/PAr5) or 55 (GAr55/PAr55) of ErbB-2. When dissociated from the membrane with geldanamycin, E2-GAr5 and E2-PAr5 were not protected and still ubiquitinated and degraded by the proteasome, despite the presence of GAr. Insertional mutagenesis with GAr sequences at a.a. 55 of E2 enhanced proteasome degradation rendering E2-GAr55 and E2-PAr55 unstable on the membrane, but rescued in the cytosol by proteasome inhibitors. Immunization with E2-GAr induced antitumor immunity and CTL which lysed tumor cells expressing chimeric E2-GAr or wild-type E2 proteins, demonstrating efficient presentation through MHC I pathway. Improved understanding of the strong degradation signals in ErbB-2 may facilitate the development of anticancer agents or vaccines.

journal_name

Cell Immunol

journal_title

Cellular immunology

authors

Piechocki MP,Pilon SA,Kelly C,Wei WZ

doi

10.1006/cimm.2001.1853

subject

Has Abstract

pub_date

2001-09-15 00:00:00

pages

138-49

issue

2

eissn

0008-8749

issn

1090-2163

pii

S0008-8749(01)91853-2

journal_volume

212

pub_type

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