NEFM

NEFM
Identifiers
Aliases	NEFM , NEF3, NF-M, NFM, neurofilament, medium polypeptide, neurofilament medium
External IDs	OMIM: 162250 HomoloGene: 38041 GeneCards: NEFM
Gene location (Human)
Chr.	Chromosome 8 (human)
End	24,919,098 bp
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• microtubule binding ; • structural constituent of cytoskeleton ; • GO:0001948 protein binding ; • structural molecule activity ;
Cellular component	• neurofibrillary tangle ; • axon ; • intermediate filament ; • neurofilament ; • intermediate filament cytoskeleton ;
Biological process	• neurofilament bundle assembly ; • axon development ;
	Sources:Amigo / QuickGO
Orthologs
	4741
	n/a
	ENSG00000104722
	n/a
	P07197
	n/a
	NM_005382 ; NM_001105541
	n/a
	NP_001099011 ; NP_005373
	n/a
	Wikidata
View/Edit Human

Last updated May 16, 2021

Neurofilament medium polypeptide (NF-M) is a protein that in humans is encoded by the NEFM gene.^[3]^[4]

Function

Neurofilaments are type IV intermediate filament heteropolymers composed of light (NEFL), medium (this protein), and heavy (NEFH) chains. Neurofilaments comprise the exoskeleton and functionally maintain neuronal caliber. They may also play a role in intracellular transport to axons and dendrites. This gene encodes the medium neurofilament protein. This protein is commonly used as a biomarker of neuronal damage.^[4]

Related Research Articles

Keratin, type I cytoskeletal 10 also known as cytokeratin-10 (CK-10) or keratin-10 (K10) is a protein that in humans is encoded by the KRT10 gene. Keratin 10 is a type I keratin.

Peripherin is a type III intermediate filament protein expressed mainly in neurons of the peripheral nervous system. It is also found in neurons of the central nervous system that have projections toward peripheral structures, such as spinal motor neurons. Its size, structure, and sequence/location of protein motifs is similar to other type III intermediate filament proteins such as desmin, vimentin and glial fibrillary acidic protein. Like these proteins, peripherin can self-assemble to form homopolymeric filamentous networks, but it can also heteropolymerize with neurofilaments in several neuronal types. This protein in humans is encoded by the PRPH gene. Peripherin is thought to play a role in neurite elongation during development and axonal regeneration after injury, but its exact function is unknown. It is also associated with some of the major neuropathologies that characterize amyotropic lateral sclerosis (ALS), but despite extensive research into how neurofilaments and peripherin contribute to ALS, their role in this disease is still unidentified.

Neurofilaments (NF) are classed as type IV intermediate filaments found in the cytoplasm of neurons. They are protein polymers measuring 10 nm in diameter and many micrometers in length. Together with microtubules (~25 nm) and microfilaments (7 nm), they form the neuronal cytoskeleton. They are believed to function primarily to provide structural support for axons and to regulate axon diameter, which influences nerve conduction velocity. The proteins that form neurofilaments are members of the intermediate filament protein family, which is divided into six types based on their gene organization and protein structure. Types I and II are the keratins which are expressed in epithelia. Type III contains the proteins vimentin, desmin, peripherin and glial fibrillary acidic protein (GFAP). Type IV consists of the neurofilament proteins L, M, H and internexin. Type V consists of the nuclear lamins, and type VI consists of the protein nestin. The type IV intermediate filament genes all share two unique introns not found in other intermediate filament gene sequences, suggesting a common evolutionary origin from one primitive type IV gene.

Tropomyosin is a two-stranded alpha-helical, coiled coil protein found in actin-based cytoskeletons.

Nestin is a protein that in humans is encoded by the NES gene.

Tropomyosin alpha-1 chain is a protein that in humans is encoded by the TPM1 gene. This gene is a member of the tropomyosin (Tm) family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells.

Tropomyosin alpha-3 chain is a protein that in humans is encoded by the TPM3 gene.

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Pinin is a protein that in humans is encoded by the PNN gene.

Beta-adducin is a protein that in humans is encoded by the ADD2 gene.

LIM domain and actin-binding protein 1 is a protein that in humans is encoded by the LIMA1 gene.

Exocyst complex component 2 is a protein that in humans is encoded by the EXOC2 gene.

Tropomodulin-1 is a protein that in humans is encoded by the TMOD1 gene.

BFSP1 is a gene that encodes the protein filensin in humans.

Gigaxonin also known as kelch-like protein 16 is a protein that in humans is encoded by the GAN gene.

Solute carrier organic anion transporter family member 1A2 is a protein that in humans is encoded by the SLCO1A2 gene.

Microtubule-associated protein 6 (MAP6) or stable tubule-only polypeptide is a protein that in humans is encoded by the MAP6 gene.

Lamin-B1 is a protein that in humans is encoded by the LMNB1 gene.

Neurofilament light polypeptide, also known as neurofilament light chain, is a neurofilament protein that in humans is encoded by the NEFL gene. Neurofilament light chain is a biomarker that can be measured with immunoassays in cerebrospinal fluid and plasma and reflects axonal damage in a wide variety of neurological disorders. It is a useful marker for disease monitoring in amyotrophic lateral sclerosis, multiple sclerosis, Alzheimer's disease, and more recently Huntington's disease. Higher numbers have been associated with increased mortality.

Keratin, type I cytoskeletal 23 is a protein that in humans is encoded by the KRT23 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000104722 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Ding Y, Reed DR, Baltazar MC, Price RA (May 1992). "RFLP for BgI II at the human neurofilament medium chain (NEF3) gene locus". Nucleic Acids Res. 20 (6): 1429. doi:10.1093/nar/20.6.1429-a. PMC 312205 . PMID 1348579.
1 2 "Entrez Gene: NEFM neurofilament, medium polypeptide 150kDa".

Xu ZS, Liu WS, Willard MB (1992). "Identification of six phosphorylation sites in the COOH-terminal tail region of the rat neurofilament protein M.". J. Biol. Chem. 267 (7): 4467–71. doi:10.1016/S0021-9258(18)42856-6. PMID 1537832.
Lee VM, Otvos L, Carden MJ, et al. (1988). "Identification of the major multiphosphorylation site in mammalian neurofilaments". Proc. Natl. Acad. Sci. U.S.A. 85 (6): 1998–2002. Bibcode:1988PNAS...85.1998L. doi:10.1073/pnas.85.6.1998. PMC 279909 . PMID 2450354.
Chin TK, Harding SE, Eagles PA (1990). "Characterization of two proteolytically derived soluble polypeptides from the neurofilament triplet components NFM and NFH". Biochem. J. 264 (1): 53–60. doi:10.1042/bj2640053. PMC 1133546 . PMID 2557834.
Myers MW, Lazzarini RA, Lee VM, et al. (1987). "The human mid-size neurofilament subunit: a repeated protein sequence and the relationship of its gene to the intermediate filament gene family". EMBO J. 6 (6): 1617–26. doi:10.1002/j.1460-2075.1987.tb02409.x. PMC 553533 . PMID 3608989.
Tu PH, Elder G, Lazzarini RA, et al. (1995). "Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits". J. Cell Biol. 129 (6): 1629–40. doi:10.1083/jcb.129.6.1629. PMC 2291190 . PMID 7790359.
Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, et al. (1995). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
Dong DL, Xu ZS, Chevrier MR, et al. (1993). "Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M.". J. Biol. Chem. 268 (22): 16679–87. doi:10.1016/S0021-9258(19)85471-6. PMID 8344946.
Fleming LM, Weisgraber KH, Strittmatter WJ, et al. (1996). "Differential binding of apolipoprotein E isoforms to tau and other cytoskeletal proteins". Exp. Neurol. 138 (2): 252–60. doi:10.1006/exnr.1996.0064. PMID 8620924. S2CID 46328348.
Dong DL, Xu ZS, Hart GW, Cleveland DW (1996). "Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H". J. Biol. Chem. 271 (34): 20845–52. doi: 10.1074/jbc.271.34.20845 . PMID 8702840.
Veeranna GJ, Shetty KT, Takahashi M, et al. (2000). "Cdk5 and MAPK are associated with complexes of cytoskeletal proteins in rat brain". Brain Res. Mol. Brain Res. 76 (2): 229–36. doi:10.1016/S0169-328X(00)00003-6. PMID 10762698.
Taylor JP, Sater R, French J, et al. (2002). "Transcription of intermediate filament genes is enhanced in focal cortical dysplasia". Acta Neuropathol. 102 (2): 141–8. doi:10.1007/s004010000348. PMID 11563628. S2CID 23648593.
Wang Y, Wang Q, Wang J (2002). "[Detection of level and mutation of neurofilament mRNA in Alzheimer's disease]". Zhonghua Yi Xue Za Zhi. 82 (8): 519–22. PMID 12133495.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241 . PMID 12477932.
Bhaskar K, Shareef MM, Sharma VM, et al. (2003). "Co-purification and localization of Munc18-1 (p67) and Cdk5 with neuronal cytoskeletal proteins". Neurochem. Int. 44 (1): 35–44. doi:10.1016/S0197-0186(03)00099-8. PMID 12963086. S2CID 23783141.
Krüger R, Fischer C, Schulte T, et al. (2004). "Mutation analysis of the neurofilament M gene in Parkinson's disease". Neurosci. Lett. 351 (2): 125–9. doi:10.1016/S0304-3940(03)00903-0. PMID 14583397. S2CID 23425379.
Garcia ML, Lobsiger CS, Shah SB, et al. (2004). "NF-M is an essential target for the myelin-directed "outside-in" signaling cascade that mediates radial axonal growth". J. Cell Biol. 163 (5): 1011–20. doi:10.1083/jcb.200308159. PMC 2173620 . PMID 14662745.
Perez-Olle R, Lopez-Toledano MA, Liem RK (2004). "The G336S variant in the human neurofilament-M gene does not affect its assembly or distribution: importance of the functional analysis of neurofilament variants". J. Neuropathol. Exp. Neurol. 63 (7): 759–74. doi: 10.1093/jnen/63.7.759 . PMID 15290901.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316 . PMID 15342556.
DeGiorgis JA, Jaffe H, Moreira JE, et al. (2005). "Phosphoproteomic analysis of synaptosomes from human cerebral cortex". J. Proteome Res. 4 (2): 306–15. doi:10.1021/pr0498436. PMID 15822905.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000104722 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1348579-3] Ding Y, Reed DR, Baltazar MC, Price RA (May 1992). "RFLP for BgI II at the human neurofilament medium chain (NEF3) gene locus". Nucleic Acids Res. 20 (6): 1429. doi:10.1093/nar/20.6.1429-a. PMC 312205 . PMID 1348579.

[entrez-4] 1 2 "Entrez Gene: NEFM neurofilament, medium polypeptide 150kDa".

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NEFM

Contents

Function

Related Research Articles

References

Further reading