The ErbB family consists of four plasma membrane-bound receptor tyrosine kinases. One of which is erbB-2, and the other members being epidermal growth factor receptor, erbB-3 <unk> regulin-binding; lacks kinase domain), and erbB-4. All four contain an extracellular ligand binding domain, a transmembrane domain, and an intracellular domain that can interact with a multitude of signaling molecules and exhibit both ligand-dependent and ligand-independent activity. Notably, no ligands for<unk>  have yet been identified.<unk>  can heterodimerise with any of the other three receptors and is considered to be the preferred dimerisation partner of the other ErbB receptors. Dimerisation results in the autophosphorylation of tyrosine residues within the cytoplasmic domain of the receptors and initiates a variety of signaling pathways. Signal transduction Signaling pathways activated by<unk>  include: * mitogen-activated protein kinase (MAPK) * phosphoinositide 3-kinase (PI3K/Akt) * phospholipase C γ * protein kinase C (PKC) * Signal transducer and activator of transcription (STAT) In summary, signaling through the ErbB family of receptors promotes cell proliferation and opposes apoptosis, and therefore must be tightly regulated to prevent uncontrolled cell growth from occurring.
HER2/neu
HERG
BIM-1
TPA-023
STS-135 
AEMT-CC
BerEp4
OPS-301