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Neurogranin

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Neurogranin is a calmodulin-binding protein expressed primarily in the brain, particularly in dendritic spines, and participating in the protein kinase C signaling pathway. Neurogranin has also been identified in aortic endothelial cells and cardiomyocytes.[5][6] It is the main postsynaptic protein regulating the availability of calmodulin by binding to it in the absence of calcium.

AliasesNRGN, RC3, hng, neurogranin
External IDsOMIM: 602350; MGI: 1927184; GeneCards: NRGN
End124,747,210 bp[1]
Quick facts NRGN, Identifiers ...
NRGN
Identifiers
AliasesNRGN, RC3, hng, neurogranin
External IDsOMIM: 602350; MGI: 1927184; GeneCards: NRGN
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006176
NM_001126181

NM_022029

RefSeq (protein)

NP_001119653
NP_006167

NP_071312

Location (UCSC)Chr 11: 124.74 – 124.75 MbChr 9: 37.46 – 37.46 Mb
PubMed search[3][4]
Wikidata
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History

Prior to its identification in bovine and rat brain in 1991,[7] neurogranin was known as a putative protein kinase C-phosphorylated protein named p17. Human neurogranin was cloned in 1997 and was found to be 96% identical to the rat protein.[8]

Structure

Human neurogranin is a small protein consisting of 78 amino acids.[8] Neurogranin belongs to a family of neuron-enriched calmodulin-binding proteins, together with neuromodulin (GAP-43), sharing a conserved central motif that functions both as the protein kinase C phosphorylation site and the calmodulin-binding domain.[7]

The protein contains an IQ motif (consensus sequence IQXXXRGXXXR), a characteristic sequence found in several calmodulin-binding proteins that mediates preferential binding to apo-calmodulin (calcium-free calmodulin). Phosphorylation of this region by protein kinase C reduces the affinity of neurogranin for calmodulin and modulates its signaling properties.[7]

Function

Neurogranin regulates intracellular calmodulin availability and functions as a key component of protein kinase C signaling. It preferentially binds calmodulin in the absence of calcium, whereas phosphorylation by protein kinase C reduces its calmodulin-binding capacity.

Expression of the NRGN gene is regulated by thyroid hormones through a thyroid hormone-responsive element located in the first intron.[9]

Recent studies suggest that neurogranin also contributes to cardiovascular physiology. In cardiomyocytes it regulates calcium-dependent cardiac hypertrophy,[10] and in endothelial cells it influences mitochondrial function and redox balance.[11]

Clinical significance

Genetic and neuropathological evidence has implicated neurogranin in schizophrenia. One study reported an association between variation in the NRGN gene and increased risk of schizophrenia in males,[12] while another demonstrated reduced neurogranin immunoreactivity in the prefrontal cortex of affected individuals.[13]

Neurogranin concentration in cerebrospinal fluid (CSF) has been investigated as a marker of synaptic dysfunction in age-related neurodegeneration.[14] CSF neurogranin has been shown to be increased in patients with Alzheimer's disease.[15][16] In particular, the ratio of CSF neurogranin truncated at P75 to the beta-secretase BACE1 has been proposed as a potential marker of cognitive deterioration during progression of Alzheimer's disease.[17]

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