ErbB-4: mechanism of action and biology.

@article{Carpenter2003ErbB4MO,
  title={ErbB-4: mechanism of action and biology.},
  author={G. Carpenter},
  journal={Experimental cell research},
  year={2003},
  volume={284 1},
  pages={
          66-77
        }
}
  • G. Carpenter
  • Published 2003
  • Biology, Medicine
  • Experimental cell research
The most recently described member of the ErbB receptor tyrosine kinase family is ErbB-4. In general, the structure of this receptor and its mechanism of action is similar to that described for ErbB-1. However, significantly less is known about ErbB-4 and there are several novel aspects to its structure, mechanism of action, and biology. This includes the spectrum of ligands that activate ErbB-4, the presence of functionally distinct isoforms, a proteolytic processing pathway to the nucleus… Expand
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References

SHOWING 1-10 OF 176 REFERENCES
Roles of ErbB-3 and ErbB-4 in the Physiology and Pathology of the Mammary Gland
TLDR
Characterization of the signaling pathways for these receptors is still incomplete, but phosphatidylinositol 3-kinase and SHC have been implicated. Expand
The cellular response to neuregulins is governed by complex interactions of the erbB receptor family
TLDR
The results provide the first comprehensive analysis of the response of this receptor family to a single peptide agonist and demonstrate the existence of several previously undocumented receptor interactions driven by neuregulin. Expand
ErbB Tyrosine Kinases and the Two Neuregulin Families Constitute a Ligand-Receptor Network
TLDR
It is concluded that the NRG-ErbB network represents a complex and nonredundant machinery developed for fine-tuning of signal transduction. Expand
Constitutive Proteolysis of the ErbB-4 Receptor Tyrosine Kinase by a Unique, Sequential Mechanism
TLDR
A unique pathway for the processing of growth factor receptors is described, which involves the sequential function of an exofacial metalloprotease and the cytoplasmic proteasome. Expand
Neuregulin-4: a novel growth factor that acts through the ErbB-4 receptor tyrosine kinase
TLDR
The primary structure and the pattern of expression of NRG-4 suggest a physiological role distinct from that of the known ErbB ligands, as well as the strict specificity of this growth factor to ErbbB-4. Expand
ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms.
Neu differentiation factor (NDF or heregulin) elevates tyrosine phosphorylation of the ErbB-2 receptor tyrosine kinase, and it was, therefore, thought to function as a ligand of this receptor.Expand
Selective Cleavage of the Heregulin Receptor ErbB-4 by Protein Kinase C Activation*
TLDR
Results show that protein kinase C negatively regulates heregulin signaling through the ErbB-4 receptor by the activation of a selective proteolytic mechanism. Expand
Neuregulin-2, a new ligand of ErbB3/ErbB4-receptor tyrosine kinases
TLDR
The results indicate that NRG-1 andNRG-2 mediate distinct biological processes by acting at different sites in tissues and eliciting different biochemical responses in cells. Expand
Erbb4 and its isoforms: selective regulation of growth factor responses by naturally occurring receptor variants.
TLDR
Four naturally occurring receptor variants provide a new level of diversity to the control of growth factor-stimulated cellular responses and may have distinct and specific roles in the regulation of various developmental and pathological processes. Expand
A Natural ErbB4 Isoform That Does Not Activate Phosphoinositide 3-Kinase Mediates Proliferation but Not Survival or Chemotaxis*
TLDR
The results suggest a novel mechanism by which cellular responses such as chemotaxis and survival may be regulated by the expression of alternative receptor-tyrosine kinase isoforms that differ in their coupling to PI3-K signaling. Expand
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