Heregulin-dependent activation of phosphoinositide 3-kinase and Akt via the ErbB2/ErbB3 co-receptor.
AuthorsHellyer NJ, Kim MS, Koland JG
JournalJ Biol Chem
PubMed ID11546794
'The ErbB2/ErbB3 heregulin co-receptor has been shown to couple to phosphoinositide (PI) 3-kinase in a heregulin-dependent manner. The recruitment and activation of PI 3-kinase by this co-receptor is presumed to occur via its interaction with phosphorylated Tyr-Xaa-Xaa-Met (YXXM) motifs occurring in the ErbB3 C terminus. In this study, mutant ErbB3 ... More
Mutational activation of ErbB2 reveals a new protein kinase autoinhibition mechanism.
AuthorsFan YX, Wong L, Ding J, Spiridonov NA, Johnson RC, Johnson GR
JournalJ Biol Chem
PubMed ID18039657
'Autoinhibition plays a key role in the control of protein kinase activity. ErbB2 is a unique receptor-tyrosine kinase that does not bind ligand but possesses an extracellular domain poised to engage other ErbBs. Little is known about the molecular mechanism for ErbB2 catalytic regulation. Here we show that ErbB2 kinase ... More
Similarity of protein encoded by the human c-erb-B-2 gene to epidermal growth factor receptor.
AuthorsYamamoto T, Ikawa S, Akiyama T, Semba K, Nomura N, Miyajima N, Saito T, Toyoshima K
JournalNature
PubMed ID3003577
'A novel v-erb-B-related gene, c-erb-B-2, which has been identified in the human genome, maps to human chromosome 17 at q21 (ref. 40), and seems to encode a polypeptide with a kinase domain that is highly homologous with, but distinct from, that of the epidermal growth factor (EGF) receptor. The c-erb-B-2 ... More
Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer cells.
'HER2/neu, a Mr 185,000 tyrosine kinase receptor that is overexpressed in breast cancer, undergoes proteolytic cleavage of its extracellular domain (ECD). In contrast with other membrane-bound proteins, including growth factor receptors, that are cleaved by a common machinery system, we show that HER2 cleavage is a slow process and is ... More
The ErbB-2/HER2 oncogenic receptor of adenocarcinomas: from orphanhood to multiple stromal ligands.
AuthorsTzahar E, Yarden Y
JournalBiochim Biophys Acta
PubMed ID9540810
Extensive clinical and biochemical evidence implicates ErbB-2, a transmembrane tyrosine kinase related to growth factor receptors, in the development, metastasis, and resistance to therapy of multiple, common human carcinomas. Previous attempts to uncover an ErbB-2-specific ligand led to isolation of the neuregulin (NRG) family, but these ligands, like all other ... More