Netrin-G1 (NTNG1) is a member of a conserved family of proteins that act as axon guidance cues during vertebrate nervous system development. Netrin-G1 contains one laminin EGF-like domain and one laminin N-terminal domain, Netrin-G1 is highly expressed in the thalamus, lowly in other tissue. Netrin-G1 localizes to the cell membrane. Netrin-G1 interacts with NGL1 and is glycosylated in the N-terminal. In addition, Netrin-G1 can promotesneurite outgrowth of both axons and dendrites.
Neuregulin 1 or NRG1 is one of four proteins in the neuregulin family that act on the EGFR family of receptors. This growth factor was originally identified as a 44-kD glycoprotein that interacts with the NEU / ERBB2 receptor tyrosine kinase to increase its phosphorylation on tyrosine residues. NRG1 is a trophic factor that has been implicated in neural development; neurotransmission; and synaptic plasticity. NRG1 has multiple isoforms that are generated by usage of different promoters and alternative splicing of a single gene. Neuregulin 1 (NRG1) is essential for the development and function of multiple organ systems; and its dysregulation has been linked to diseases such as cancer and schizophrenia. NRG1 is a schizophrenia candidate gene and plays an important role in brain development and neural function. Schizophrenia is a complex disorder; with etiology likely due to epistasis.
Neurexophilin-1 (NXPH1) is a member of Neurexophilin family. NXPH1 consist of 271 amino acis. It contains a 21 amino acid signal peptide, 86 amino acid propeptide, and 164 amino acid mature protein. NXPH1 is expressed in subpopulations of neurons within the cerebral cortex, cerebellum and olfactory bulb that are thought to be inhibitory interneurons. In humans, NXPH2 and NXPH3 are most similar to NXPH1, sharing 84% and 64% aa identity within the mature region, respectively. By contrast, NXPH4 dost not bind a-neurexins. Genetic deletion of NXPH1 or NXPH3 produces no anatomical effect.
Neuritin 1 (NRN1) is a member of neuritin family. Neuritin is a glycosylphosphatidylinositol- anchored protein induced by neural activity. It is expressed in postmitotic-differentiating neurons of the developing nervous system and a population of small-diameter neurons in the dorsal root ganglia and was anterogradely and retrogradely transported. Neuritin message is induced by neuronal activity and by the activity-regulated neurotrophins BDNF; nerve growth factor (NGF) and NT-3. Purified recombinant neuritin promotes neurite outgrowth and arborization in primary embryonic hippocampal and cortical cultures. Thus; neuritin is considered as a downstream effector of activity-induced neurite outgrowth. In clinical; neuritin levels in diabetes were reduced in both dorsal root ganglia and sciatic nerve of rats; and these deficits were reversed in vivo by treatment with NGF. This manipulation of neuritin levels in diabetes may provide a potential target for the therapeutic intervention in the management of neuropathy.
Neuritin/NRN1 is a member of the neuritin family and can be expressed in postmitotic-differentiating neurons of the developmental nervous system and neuronal structures associated with plasticity in the adult. Neuritin/NRN1 promotes neurite outgrowt; arborization and neuritogenesis. The protein contains a consensus cleavage signal found in glycosylphoshatidylinositol (GPI)-anchored proteins.Overexpression of the encoded protein may be associated with astrocytoma progression.
Neurocalcin-delta (NCALD) is a neuronal calcium-binding protein that belongs to the neuronal calcium sensor (NCS) family. It expressed in mammalian brains. NCALD contains an N-terminal myristoylation signal and four EF-hand calcium binding loops. The protein possesses a Ca2+ /myristoyl switch. It is cytosolic at resting calcium levels. However, elevated intracellular calcium levels induce a conformational change which exposes the myristoyl group, resulting in protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is thought to be a regulator of G protein-coupled receptor signal transduction.
Neuroligin 1 (NLGN1) belongs to the type-B carboxylesterase/lipase family; is a synaptic cell-adhesion molecule that is enriched in postsynaptic densities where it may recruit receptors; channels; and signal-transduction molecules to synaptic sites of cell adhesion. Neuroligins consist of five members (NLGN1; NLGN2; NLGN3; NLGN4 and NLGN4Y); which interact with beta-neurexins and this interaction is involved in the formation of functional synapses. The extracellular domain of functional Neuroligin 1 associates as a dimer when analyzed by sedimentation equilibrium. Neuroligin 1 has a unique N-linked glycosylation pattern in the neuroligin family; and glycosylation and its processing modify neuroligin activity. Neuroligin 1 is a potent trigger for the de novo formation of synaptic connections; and it has recently been suggested that it is required for the maturation of functionally competent excitatory synapses. The persistent expression of Neuroligin 1 is required for the maintenance of NMDAR-mediated synaptic transmission; which enables normal development of synaptic plasticity and long-term memory in the amygdala of adult animals.
Neuroligin-1 is a single-pass type I transmembrane protein which belongs to the type-B Carboxylesterase/Lipase family. Neuroligins are cell-adhesion molecules located at the postsynaptic side of the synapse. Neuroligins interact with beta-neurexins and this interaction is involved in the formation of functional synapses. Neurexins and Neuroligins are cell adhesion molecules present in excitatory and inhibitory synapses, and they are required for correct neuron network function. These proteins are found at the presynaptic and postsynaptic membranes. Neuroligin-1 is a neuronal cell surface protein which is thought to be involved in cell-cell-interactions by forming intercellular junctions through binding to beta-neurexins. It seems to play role in formation or maintenance of synaptic junctions. It triggers the de novo formation of presynaptic structures and may be involved in specification of excitatory synapses.
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