描述：
The neuregulin family of structurally related glycoproteins comprises products from four
distinct but related genes, Nrg-1, Nrg-2, Nrg-3, and Nrg-4. Through alternative splicing or
the use of alternative promoters, Nrg-1 encodes more than 14 soluble or transmembrane
proteins. The extracellular domain of the transmembrane NRG1 isoforms can be proteolytically
cleaved to release soluble growth factors. The α-or β-splice variants differ in their C-terminal
region. All NRG1 isoforms contain an EGF-like domain that is required for their direct binding
to the ErbB3 or ErbB4 receptor tyrosine kinases. The ErbB3 or ErbB4 subsequently recruits
and heterodimerizes with ErbB2, resulting in tyrosine phosphorylation and NRG1 signaling.
NRG1 isoforms can be classified into three major subtypes. Type I (Neu Differentiation Factor,
NDF; Heregulin, HRG; Acetylcholine Receptor Inducing Activity, ARIA) and type II (Glial Growth
Factor, GGF). NRG1s have an immunoglobulin (Ig)-like domain N-terminal to the EGF-like
domain. Type I NRG1s differ from type II NRG1s by having a glycosylationrich domain between
the Iglike and the EGF-like domains. Type III NRG1 (Sensory and Motor neuronDerived Factor)
lacks the Iglike domain but has a cysteine rich domain (CRD) instead. NRG1 isoforms show
distinct spatial and temporal expression patterns. These proteins play important roles during
development of both the nervous system and the heart. They have been shown to regulate
the selective expression of neurotransmitter receptors in neurons and at the neuromuscular
junction, and to promote the differentiation and development of Schwann cells from neural
crest stem cells. NRG1s have also been shown to be involved in the establishment of the
oligodendroglial lineage.
原厂资料：
The neuregulin family of structurally related glycoproteins comprises products from four
distinct but related genes, Nrg-1, Nrg-2, Nrg-3, and Nrg-4. Through alternative splicing or
the use of alternative promoters, Nrg-1 encodes more than 14 soluble or transmembrane
proteins. The extracellular domain of the transmembrane NRG1 isoforms can be proteolytically
cleaved to release soluble growth factors. The α-or β-splice variants differ in their C-terminal
region. All NRG1 isoforms contain an EGF-like domain that is required for their direct binding
to the ErbB3 or ErbB4 receptor tyrosine kinases. The ErbB3 or ErbB4 subsequently recruits
and heterodimerizes with ErbB2, resulting in tyrosine phosphorylation and NRG1 signaling.
NRG1 isoforms can be classified into three major subtypes. Type I (Neu Differentiation Factor,
NDF; Heregulin, HRG; Acetylcholine Receptor Inducing Activity, ARIA) and type II (Glial Growth
Factor, GGF). NRG1s have an immunoglobulin (Ig)-like domain N-terminal to the EGF-like
domain. Type I NRG1s differ from type II NRG1s by having a glycosylationrich domain between
the Iglike and the EGF-like domains. Type III NRG1 (Sensory and Motor neuronDerived Factor)
lacks the Iglike domain but has a cysteine rich domain (CRD) instead. NRG1 isoforms show
distinct spatial and temporal expression patterns. These proteins play important roles during
development of both the nervous system and the heart. They have been shown to regulate
the selective expression of neurotransmitter receptors in neurons and at the neuromuscular
junction, and to promote the differentiation and development of Schwann cells from neural
crest stem cells. NRG1s have also been shown to be involved in the establishment of the
oligodendroglial lineage.
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