The neuregulins, including NRG4, activate type-1 growth factor receptors (see EGFR; MIM 131550) to initiating cell-to-cell signaling through tyrosine phosphorylation (Harari et al., 1999 [PubMed 10348342]).[supplied by OMIM, Mar 2008],
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Function:
Domain:ERBB receptor binding is elicited entirely by the EGF-like domain.,Domain:The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization.,Function:Low affinity ligand for the ERBB4 tyrosine kinase receptor. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. Does not bind to the ERBB1, ERBB2 and ERBB3 receptors.,PTM:Extensive glycosylation precedes the proteolytic cleavage.,PTM:Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form.,similarity:Belongs to the neuregulin family.,similarity:Contains 1 EGF-like domain.,subcellular location:Does not seem to be active.,
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Cellular Localization:
[Pro-neuregulin-4, membrane-bound isoform]: Cell membrane ; Single-pass type I membrane protein . Does not seem to be active. .; [Neuregulin-4]: Secreted .