Neurogranin

Last updated
NRGN
Identifiers
Aliases NRGN , RC3, hng, neurogranin
External IDs OMIM: 602350 HomoloGene: 136802 GeneCards: NRGN
Orthologs
SpeciesHumanMouse
Entrez

4900

n/a

Ensembl

ENSG00000154146

n/a

UniProt

Q92686

n/a

RefSeq (mRNA)

NM_006176
NM_001126181

n/a

RefSeq (protein)

NP_001119653
NP_006167

n/a

Location (UCSC) Chr 11: 124.74 – 124.75 Mb n/a
PubMed search [2] n/a
Wikidata
View/Edit Human
neurogranin (protein kinase C substrate, RC3)
Identifiers
SymbolNRGN
NCBI gene 4900
HGNC 8000
OMIM 602350
RefSeq NM_006176
UniProt Q92686
Other data
Locus Chr. 11 q24
Search for
Structures Swiss-model
Domains InterPro

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 recently been found in aortic endothelial cells and cardiomyocytes. [3] [4] Neurogranin is the main postsynaptic protein regulating the availability of calmodulin, binding to it in the absence of calcium. Phosphorylation by protein kinase C lowers its binding ability. NRGN gene expression is controlled by thyroid hormones. [5] Human neurogranin consists of 78 amino acids.

One study tells of potential link of neurogranin gene to the heightened risk of schizophrenia in males, [6] another study gives evidence of lowered neurogranin immunoreactivity in the brains of people suffering from schizophrenia. [7]

Neurogranin concentration in cerebrospinal fluid (CSF) is further discussed as marker for synaptic dysfunction in age-related neurodegeneration. [8] It has also been shown to be specifically increased in patients with Alzheimer's disease. [9] [10] Especially the ratio of CSF neurogranin trunc P75 and the beta-secretase BACE1 is suggested as potential marker for cognitive deterioration in the progress of Alzheimer's disease. [11]

Prior to its identification in the bovine and rat brain in 1991, [12] neurogranin was known as a putative protein kinase C-phosphorylated protein named p17. Human neurogranin was cloned in 1997 and turned out to be 96% identical to the rat protein. [13]

Related Research Articles

<span class="mw-page-title-main">Calmodulin</span> Messenger protein

Calmodulin (CaM) (an abbreviation for calcium-modulated protein) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of calmodulin. Once bound to Ca2+, calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases.

<span class="mw-page-title-main">CREB</span> Class of proteins

CREB-TF is a cellular transcription factor. It binds to certain DNA sequences called cAMP response elements (CRE), thereby increasing or decreasing the transcription of the genes. CREB was first described in 1987 as a cAMP-responsive transcription factor regulating the somatostatin gene.

<span class="mw-page-title-main">Calcineurin</span> Class of enzymes

Calcineurin (CaN) is a calcium and calmodulin dependent serine/threonine protein phosphatase. It activates the T cells of the immune system and can be blocked by drugs. Calcineurin activates nuclear factor of activated T cell cytoplasmic (NFATc), a transcription factor, by dephosphorylating it. The activated NFATc is then translocated into the nucleus, where it upregulates the expression of interleukin 2 (IL-2), which, in turn, stimulates the growth and differentiation of the T cell response. Calcineurin is the target of a class of drugs called calcineurin inhibitors, which include ciclosporin, voclosporin, pimecrolimus and tacrolimus.

<span class="mw-page-title-main">Transthyretin</span> Serum protein related to amyloid diseases

Transthyretin (TTR or TBPA) is a transport protein in the plasma and cerebrospinal fluid that transports the thyroid hormone thyroxine (T4) and retinol to the liver. This is how transthyretin gained its name: transports thyroxine and retinol. The liver secretes TTR into the blood, and the choroid plexus secretes TTR into the cerebrospinal fluid.

<span class="mw-page-title-main">Myosin light-chain kinase</span> Class of kinase enzymes

Myosin light-chain kinase also known as MYLK or MLCK is a serine/threonine-specific protein kinase that phosphorylates a specific myosin light chain, namely, the regulatory light chain of myosin II.

<span class="mw-page-title-main">Tyrosine hydroxylase</span> Enzyme found in Homo sapiens that converts l-tyrosine to l-dopa, the precursor of cathecolamines

Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). It does so using molecular oxygen (O2), as well as iron (Fe2+) and tetrahydrobiopterin as cofactors. L-DOPA is a precursor for dopamine, which, in turn, is a precursor for the important neurotransmitters norepinephrine (noradrenaline) and epinephrine (adrenaline). Tyrosine hydroxylase catalyzes the rate limiting step in this synthesis of catecholamines. In humans, tyrosine hydroxylase is encoded by the TH gene, and the enzyme is present in the central nervous system (CNS), peripheral sympathetic neurons and the adrenal medulla. Tyrosine hydroxylase, phenylalanine hydroxylase and tryptophan hydroxylase together make up the family of aromatic amino acid hydroxylases (AAAHs).

Calmodulin-binding proteins are, as their name implies, proteins which bind calmodulin. Calmodulin can bind to a variety of proteins through a two-step binding mechanism, namely "conformational and mutually induced fit", where typically two domains of calmodulin wrap around an emerging helical calmodulin binding domain from the target protein.

<span class="mw-page-title-main">Protein kinase R</span> Human protein and coding gene

Protein kinase RNA-activated also known as protein kinase R (PKR), interferon-induced, double-stranded RNA-activated protein kinase, or eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) is an enzyme that in humans is encoded by the EIF2AK2 gene on chromosome 2. PKR is a serine/tyrosine kinase that is 551 amino acids long.

<span class="mw-page-title-main">Calcium/calmodulin-dependent protein kinase type II subunit alpha</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type II subunit alpha (CAMKIIα), a.k.a.Ca2+/calmodulin-dependent protein kinase II alpha, is one subunit of CamKII, a protein kinase (i.e., an enzyme which phosphorylates proteins) that in humans is encoded by the CAMK2A gene.

<span class="mw-page-title-main">CALM3</span> Protein-coding gene in the species Homo sapiens

Calmodulin 3 is a protein that in humans is encoded by the CALM3 gene.

<span class="mw-page-title-main">CAMK2B</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type II beta chain is an enzyme that in humans is encoded by the CAMK2B gene.

<span class="mw-page-title-main">ATF1</span> Protein-coding gene in humans

Cyclic AMP-dependent transcription factor ATF-1 is a protein that in humans is encoded by the ATF1 gene.

<span class="mw-page-title-main">CAMK4</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type IV is an enzyme that in humans is encoded by the CAMK4 gene.

<span class="mw-page-title-main">S100B</span> Human protein and coding gene

S100 calcium-binding protein B (S100B) is a protein of the S-100 protein family.

<span class="mw-page-title-main">CAMK2G</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene.

<span class="mw-page-title-main">CAMK1</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type 1 is an enzyme that in humans is encoded by the CAMK1 gene.

<span class="mw-page-title-main">PHKG1</span> Protein-coding gene in the species Homo sapiens

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform is an enzyme that in humans is encoded by the PHKG1 gene.

<span class="mw-page-title-main">Visinin-like protein 1</span> Protein-coding gene in the species Homo sapiens

Visinin-like protein 1 is a protein that in humans is encoded by the VSNL1 gene.

<span class="mw-page-title-main">EEF2K</span> Protein-coding gene in humans

Eukaryotic elongation factor-2 kinase, also known as calmodulin-dependent protein kinase III (CAMKIII) and calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase, is an enzyme that in humans is encoded by the EEF2K gene.

<span class="mw-page-title-main">Calcium-binding protein 1</span> Protein-coding gene in the species Homo sapiens

Calcium binding protein 1 is a protein that in humans is encoded by the CABP1 gene. Calcium-binding protein 1 is a calcium-binding protein discovered in 1999. It has two EF hand motifs and is expressed in neuronal cells in such areas as hippocampus, habenular nucleus of the epithalamus, Purkinje cell layer of the cerebellum, and the amacrine cells and cone bipolar cells of the retina.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000154146 - Ensembl, May 2017
  2. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ↑ Jorgensen, Ashton N.; Abdullah, Chowdhury S.; Bhuiyan, Md. Shenuarin; Watt, Megan; Dominic, Paari; Kolluru, Gopi K.; Kevil, Christopher G.; Nam, Hyung W. (August 2022). "Neurogranin regulates calcium-dependent cardiac hypertrophy". Experimental and Molecular Pathology. 127: 104815. doi:10.1016/j.yexmp.2022.104815. PMID   35870494. S2CID   250941689.
  4. ↑ Jorgensen, Ashton N.; Rashdan, Nabil A.; Rao, K.N. Shashanka; Delgadillo, Luisa F.; Kolluru, Gopi K.; Krzywanski, David M.; Pattillo, Christopher B.; Kevil, Christopher G.; Nam, Hyung W. (April 2024). "Neurogranin expression regulates mitochondrial function and redox balance in endothelial cells". Redox Biology. 70: 103085. doi:10.1016/j.redox.2024.103085. PMC   10878108 . PMID   38359746.
  5. ↑ Martínez de Arrieta C, Morte B, Coloma A, Bernal J (January 1999). "The human RC3 gene homolog, NRGN contains a thyroid hormone-responsive element located in the first intron". Endocrinology. 140 (1): 335–43. doi: 10.1210/en.140.1.335 . hdl: 10261/24257 . PMID   9886843.
  6. ↑ Ruano D, Aulchenko YS, Macedo A, Soares MJ, Valente J, Azevedo MH, et al. (January 2008). "Association of the gene encoding neurogranin with schizophrenia in males". Journal of Psychiatric Research. 42 (2): 125–33. doi:10.1016/j.jpsychires.2006.10.008. PMID   17140601.
  7. ↑ Broadbelt K, Ramprasaud A, Jones LB (October 2006). "Evidence of altered neurogranin immunoreactivity in areas 9 and 32 of schizophrenic prefrontal cortex". Schizophrenia Research. 87 (1–3): 6–14. doi:10.1016/j.schres.2006.04.028. PMID   16797925. S2CID   38984915.
  8. ↑ Casaletto KB, Elahi FM, Bettcher BM, Neuhaus J, Bendlin BB, Asthana S, et al. (October 2017). "Neurogranin, a synaptic protein, is associated with memory independent of Alzheimer biomarkers". Neurology. 89 (17): 1782–1788. doi:10.1212/WNL.0000000000004569. PMC   5664306 . PMID   28939668.
  9. ↑ De Vos A, Jacobs D, Struyfs H, Fransen E, Andersson K, Portelius E, et al. (December 2015). "C-terminal neurogranin is increased in cerebrospinal fluid but unchanged in plasma in Alzheimer's disease". Alzheimer's & Dementia. 11 (12): 1461–1469. doi: 10.1016/j.jalz.2015.05.012 . PMID   26092348.
  10. ↑ Willemse EA, De Vos A, Herries EM, Andreasson U, Engelborghs S, van der Flier WM, et al. (June 2018). "Neurogranin as Cerebrospinal Fluid Biomarker for Alzheimer Disease: An Assay Comparison Study". Clinical Chemistry. 64 (6): 927–937. doi: 10.1373/clinchem.2017.283028 . hdl: 10067/1495100151162165141 . PMID   29523639.
  11. ↑ De Vos A, Struyfs H, Jacobs D, Fransen E, Klewansky T, De Roeck E, et al. (July 2016). "The Cerebrospinal Fluid Neurogranin/BACE1 Ratio is a Potential Correlate of Cognitive Decline in Alzheimer's Disease". Journal of Alzheimer's Disease. 53 (4): 1523–38. doi:10.3233/JAD-160227. PMC   4981899 . PMID   27392859.
  12. ↑ Baudier J, Deloulme JC, Van Dorsselaer A, Black D, Matthes HW (January 1991). "Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). Identification of a consensus amino acid sequence between neurogranin and neuromodulin (GAP43) that corresponds to the protein kinase C phosphorylation site and the calmodulin-binding domain". The Journal of Biological Chemistry. 266 (1): 229–37. doi: 10.1016/S0021-9258(18)52425-X . PMID   1824695.
  13. ↑ Martínez de Arrieta C, Pérez Jurado L, Bernal J, Coloma A (April 1997). "Structure, organization, and chromosomal mapping of the human neurogranin gene (NRGN)". Genomics. 41 (2): 243–9. doi:10.1006/geno.1997.4622. PMID   9143500.


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