Cargando…

ERBB2 oncogenicity: ERBIN helps to perform the job

ERBB2 (v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 2) is an oncogenic tyrosine kinase receptor that is overexpressed in breast cancer. Antibodies and inhibitors targeting ERBB2 are currently available, although therapeutic failures remain frequent. We discuss here recent data showi...

Descripción completa

Detalles Bibliográficos
Autores principales: Mei, Lin, Borg, Jean-Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4905317/
https://www.ncbi.nlm.nih.gov/pubmed/27308480
http://dx.doi.org/10.4161/23723556.2014.995033
_version_ 1782437246566137856
author Mei, Lin
Borg, Jean-Paul
author_facet Mei, Lin
Borg, Jean-Paul
author_sort Mei, Lin
collection PubMed
description ERBB2 (v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 2) is an oncogenic tyrosine kinase receptor that is overexpressed in breast cancer. Antibodies and inhibitors targeting ERBB2 are currently available, although therapeutic failures remain frequent. We discuss here recent data showing that the scaffold protein ERBB2IP (ERBB2 interacting protein, best known as ERBIN) regulates ERBB2 stability and may represent a future therapeutic target.
format Online
Article
Text
id pubmed-4905317
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher Taylor & Francis
record_format MEDLINE/PubMed
spelling pubmed-49053172016-06-15 ERBB2 oncogenicity: ERBIN helps to perform the job Mei, Lin Borg, Jean-Paul Mol Cell Oncol Author's Views ERBB2 (v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 2) is an oncogenic tyrosine kinase receptor that is overexpressed in breast cancer. Antibodies and inhibitors targeting ERBB2 are currently available, although therapeutic failures remain frequent. We discuss here recent data showing that the scaffold protein ERBB2IP (ERBB2 interacting protein, best known as ERBIN) regulates ERBB2 stability and may represent a future therapeutic target. Taylor & Francis 2015-03-19 /pmc/articles/PMC4905317/ /pubmed/27308480 http://dx.doi.org/10.4161/23723556.2014.995033 Text en © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Author's Views
Mei, Lin
Borg, Jean-Paul
ERBB2 oncogenicity: ERBIN helps to perform the job
title ERBB2 oncogenicity: ERBIN helps to perform the job
title_full ERBB2 oncogenicity: ERBIN helps to perform the job
title_fullStr ERBB2 oncogenicity: ERBIN helps to perform the job
title_full_unstemmed ERBB2 oncogenicity: ERBIN helps to perform the job
title_short ERBB2 oncogenicity: ERBIN helps to perform the job
title_sort erbb2 oncogenicity: erbin helps to perform the job
topic Author's Views
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4905317/
https://www.ncbi.nlm.nih.gov/pubmed/27308480
http://dx.doi.org/10.4161/23723556.2014.995033
work_keys_str_mv AT meilin erbb2oncogenicityerbinhelpstoperformthejob
AT borgjeanpaul erbb2oncogenicityerbinhelpstoperformthejob