EIF2B2

In today's world, EIF2B2 has gained impressive relevance. Whether in the field of technology, health, politics or entertainment, EIF2B2 has managed to capture the attention of millions of people around the world. Its impact has been felt significantly, generating both enthusiasm and controversy. In this article, we will thoroughly explore the phenomenon of EIF2B2, from its origins to its influence on today's society. Through a detailed analysis, we will discover how EIF2B2 has transformed the way we think, interact, and perceive the world around us.

Protein-coding gene in the species Homo sapiens

EIF2B2
Identifiers
Aliases	EIF2B2, EIF-2Bbeta, EIF2B, eukaryotic translation initiation factor 2B subunit beta, EIF2Bbeta
External IDs	OMIM: 606454; MGI: 2145118; HomoloGene: 6507; GeneCards: EIF2B2; OMA:EIF2B2 - orthologs
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q24.3 Start 75,002,921 bp[1] End 75,012,366 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12|12 D1 Start 85,266,255 bp[2] End 85,273,402 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left lobe of thyroid gland right lobe of thyroid gland right adrenal cortex gastrocnemius muscle left adrenal gland muscle of thigh left adrenal cortex popliteal artery tibial arteries mucosa of transverse colon Top expressed in condyle fossa renal corpuscle internal carotid artery external carotid artery endocardial cushion saccule yolk sac substantia nigra medullary collecting duct More reference expression data BioGPS More reference expression data
Gene ontology Molecular function translation initiation factor activity guanyl-nucleotide exchange factor activity GTP binding protein binding ATP binding Cellular component cytoplasm cytosol eukaryotic translation initiation factor 2B complex Biological process response to peptide hormone response to heat response to glucose central nervous system development cell metabolism ovarian follicle development myelination oligodendrocyte development regulation of translational initiation protein biosynthesis translational initiation T cell receptor signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8892 217715 Ensembl ENSG00000119718 ENSMUSG00000004788 UniProt P49770 Q99LD9 RefSeq (mRNA) NM_014239 NM_145445 RefSeq (protein) NP_055054 NP_663420 Location (UCSC) Chr 14: 75 – 75.01 Mb Chr 12: 85.27 – 85.27 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Translation initiation factor eIF-2B subunit beta is a protein that in humans is encoded by the EIF2B2 gene.^[5][6]

Function

Eukaryotic initiation factor-2B (EIF2B) is a GTP exchange protein essential for protein synthesis. It consists of alpha (EIF2B1; MIM 606686), beta (EIF2B2), gamma (EIF2B3; MIM 606273), delta (EIF2B4; MIM 606687), and epsilon (EIF2B5; MIM 603945) subunits. EIF2B activates its EIF2 (see MIM 603907) substrate by exchanging EIF2-bound GDP for GTP.^[6]

Interactions

EIF2B2 has been shown to interact with EIF2B5^[7] and NCK1.^[8]

References

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000119718 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000004788 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Yang W, Hinnebusch AG (December 1996). "Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2". Mol Cell Biol. 16 (11): 6603–16. doi:10.1128/MCB.16.11.6603. PMC 231662. PMID 8887689.
6. ^ ^{a b} "Entrez Gene: EIF2B2 eukaryotic translation initiation factor 2B, subunit 2 beta, 39kDa".
7. ^ Anthony TG, Fabian JR, Kimball SR, Jefferson LS (June 2000). "Identification of domains within the epsilon-subunit of the translation initiation factor eIF2B that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation". Biochim. Biophys. Acta. 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2. PMID 10858531.
8. ^ Kebache S, Zuo D, Chevet E, Larose L (April 2002). "Modulation of protein translation by Nck-1". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5406–5411. Bibcode:2002PNAS...99.5406K. doi:10.1073/pnas.082483399. PMC 122782. PMID 11959995.

Further reading

• Labauge P, Fogli A, Niel F, Rodriguez D, Boespflug-Tanguy O (2007). "". Rev. Neurol. (Paris). 163 (8–9): 793–9. doi:10.1016/s0035-3787(07)91461-7. PMID 17878805.
• Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, Tsuda T, Mar L, Foncin JF, Bruni AC, Montesi MP, Sorbi S, Rainero I, Pinessi L, Nee L, Chumakov I, Pollen D, Brookes A, Sanseau P, Polinsky RJ, Wasco W, Da Silva HA, Haines JL, Perkicak-Vance MA, Tanzi RE, Roses AD, Fraser PE, Rommens JM, St George-Hyslop PH (1995). "Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease". Nature. 375 (6534): 754–760. Bibcode:1995Natur.375..754S. doi:10.1038/375754a0. PMID 7596406. S2CID 4308372.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–113. doi:10.1006/abio.1996.0138. PMID 8619474.
• Welsh GI, Miyamoto S, Price NT, Safer B, Proud CG (1996). "T-cell activation leads to rapid stimulation of translation initiation factor eIF2B and inactivation of glycogen synthase kinase-3". J. Biol. Chem. 271 (19): 11410–11413. doi:10.1074/jbc.271.19.11410. PMID 8626696.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Kimball SR, Heinzinger NK, Horetsky RL, Jefferson LS (1998). "Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B". J. Biol. Chem. 273 (5): 3039–3044. doi:10.1074/jbc.273.5.3039. PMID 9446619.
• Gomez E, Pavitt GD (2000). "Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation". Mol. Cell. Biol. 20 (11): 3965–3976. doi:10.1128/MCB.20.11.3965-3976.2000. PMC 85753. PMID 10805739.
• Anthony TG, Fabian JR, Kimball SR, Jefferson LS (2000). "Identification of domains within the epsilon-subunit of the translation initiation factor eIF2B that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation". Biochim. Biophys. Acta. 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2. PMID 10858531.
• Williams DD, Price NT, Loughlin AJ, Proud CG (2001). "Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein". J. Biol. Chem. 276 (27): 24697–24703. doi:10.1074/jbc.M011788200. PMID 11323413.
• Leegwater PA, Vermeulen G, Könst AA, Naidu S, Mulders J, Visser A, Kersbergen P, Mobach D, Fonds D, van Berkel CG, Lemmers RJ, Frants RR, Oudejans CB, Schutgens RB, Pronk JC, van der Knaap MS (2001). "Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter". Nat. Genet. 29 (4): 383–388. doi:10.1038/ng764. PMID 11704758. S2CID 20313523.
• Kebache S, Zuo D, Chevet E, Larose L (2002). "Modulation of protein translation by Nck-1". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5406–5411. Bibcode:2002PNAS...99.5406K. doi:10.1073/pnas.082483399. PMC 122782. PMID 11959995.
• Fogli A, Dionisi-Vici C, Deodato F, Bartuli A, Boespflug-Tanguy O, Bertini E (2003). "A severe variant of childhood ataxia with central hypomyelination/vanishing white matter leukoencephalopathy related to EIF21B5 mutation". Neurology. 59 (12): 1966–8. doi:10.1212/01.wnl.0000041666.76863.47. PMID 12499492. S2CID 13129517.
• Fogli A, Rodriguez D, Eymard-Pierre E, Bouhour F, Labauge P, Meaney BF, Zeesman S, Kaneski CR, Schiffmann R, Boespflug-Tanguy O (2003). "Ovarian failure related to eukaryotic initiation factor 2B mutations". Am. J. Hum. Genet. 72 (6): 1544–1550. doi:10.1086/375404. PMC 1180314. PMID 12707859.
• van der Knaap MS, van Berkel CG, Herms J, van Coster R, Baethmann M, Naidu S, Boltshauser E, Willemsen MA, Plecko B, Hoffmann GF, Proud CG, Scheper GC, Pronk JC (2004). "eIF2B-related disorders: antenatal onset and involvement of multiple organs". Am. J. Hum. Genet. 73 (5): 1199–1207. doi:10.1086/379524. PMC 1180499. PMID 14566705.
• Richardson JP, Mohammad SS, Pavitt GD (2004). "Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity". Mol. Cell. Biol. 24 (6): 2352–2363. doi:10.1128/MCB.24.6.2352-2363.2004. PMC 355856. PMID 14993275.
• Fogli A, Schiffmann R, Hugendubler L, Combes P, Bertini E, Rodriguez D, Kimball SR, Boespflug-Tanguy O (2005). "Decreased guanine nucleotide exchange factor activity in eIF2B-mutated patients". Eur. J. Hum. Genet. 12 (7): 561–566. doi:10.1038/sj.ejhg.5201189. PMID 15054402.
• Li W, Wang X, Van Der Knaap MS, Proud CG (2004). "Mutations linked to leukoencephalopathy with vanishing white matter impair the function of the eukaryotic initiation factor 2B complex in diverse ways". Mol. Cell. Biol. 24 (8): 3295–3306. doi:10.1128/MCB.24.8.3295-3306.2004. PMC 381664. PMID 15060152.

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