GJA8

Gap junction protein, alpha 8, 50kDa

Identifiers

GJA8 ; CAE; CAE1; CTRCT1; CX50; CZP1; MP70

External IDs

OMIM: 600897 MGI: 99953 HomoloGene: 3857 IUPHAR: 732 GeneCards: GJA8 Gene

Gene ontology
Molecular function	• gap junction channel activity • channel activity
Cellular component	• integral component of plasma membrane • connexon complex
Biological process	• lens development in camera-type eye • transport • cell-cell signaling • visual perception • protein homooligomerization • transmembrane transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
147.91 – 147.91 Mb

Chr 3:
96.91 – 96.93 Mb

PubMed search

Connexin50

Identifiers

Symbol

Connexin50

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Gap junction alpha-8 protein is a protein that in humans is encoded by the GJA8 gene.^[1]^[2]^[3] It is also known as connexin 50.

Interactions

GJA8 has been shown to interact with Tight junction protein 1.^[6]

References

↑ Shiels A, Mackay D, Ionides A, Berry V, Moore A, Bhattacharya S (Apr 1998). "A missense mutation in the human connexin50 gene (GJA8) underlies autosomal dominant "zonular pulverulent" cataract, on chromosome 1q". Am J Hum Genet 62 (3): 526–32. doi:10.1086/301762. PMC 1376956. PMID 9497259.
↑ Church RL, Wang JH, Steele E (Aug 1995). "The human lens intrinsic membrane protein MP70 (Cx50) gene: clonal analysis and chromosome mapping". Curr Eye Res 14 (3): 215–21. doi:10.3109/02713689509033517. PMID 7796604.
↑ "Entrez Gene: GJA8 gap junction protein, alpha 8, 50kDa".
1 2 Mefford HC, Sharp AJ, Baker C, Itsara A, Jiang Z, Buysse K, Huang S, Maloney VK, Crolla JA, Baralle D; et al. (October 2008). "Recurrent rearrangements of chromosome 1q21.1 and variable pediatric phenotypes". N. Engl. J. Med. 359 (16): 1685–99. doi:10.1056/NEJMoa0805384. PMC 2703742. PMID 18784092.
↑ Rong P, Wang X, Niesman I, Wu Y, Benedetti LE, Dunia I, Levy E, Gong X (January 2002). "Disruption of Gja8 (alpha8 connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation". Development 129 (1): 167–74. PMID 11782410.
↑ Nielsen PA, Baruch A, Shestopalov VI, Giepmans BN, Dunia I, Benedetti EL, Kumar NM (June 2003). "Lens connexins alpha3Cx46 and alpha8Cx50 interact with zonula occludens protein-1 (ZO-1)". Mol. Biol. Cell 14 (6): 2470–81. doi:10.1091/mbc.E02-10-0637. PMC 194895. PMID 12808044.

Andrew L Harris and Darren Locke (2009). Connexins, A Guide. New York: Springer. p. 574. ISBN 978-1-934115-46-6.
Cook PJ, Hamerton JL (1980). "Report of the committee on the genetic constitution of chromosome 1.". Cytogenet. Cell Genet. 25 (1-4): 9–20. doi:10.1159/000131394. PMID 396131.
Jarvis LJ, Louis CF (1993). "The permeability of reconstituted liposomes containing the purified lens fiber cell integral membrane proteins MP20, MP26 and MP70.". J. Membr. Biol. 130 (3): 251–63. doi:10.1007/bf00240482. PMID 1491428.
Church RL, Wang JH, Steele E (1996). "The human lens intrinsic membrane protein MP70 (Cx50) gene: clonal analysis and chromosome mapping.". Curr. Eye Res. 14 (10): 979–81. doi:10.3109/02713689508995138. PMID 8549164.
Geyer DD, Church RL, Steele EC; et al. (1998). "Regional mapping of the human MP70 (Cx50; connexin 50) gene by fluorescence in situ hybridization to 1q21.1.". Mol. Vis. 3: 13. PMID 9479004.
Dunia I, Recouvreur M, Nicolas P; et al. (1998). "Assembly of connexins and MP26 in lens fiber plasma membranes studied by SDS-fracture immunolabeling.". J. Cell. Sci. 111 (15): 2109–20. PMID 9664032.
Hopperstad MG, Srinivas M, Spray DC (2000). "Properties of gap junction channels formed by Cx46 alone and in combination with Cx50.". Biophys. J. 79 (4): 1954–66. doi:10.1016/S0006-3495(00)76444-7. PMC 1301086. PMID 11023900.
Xu X, Berthoud VM, Beyer EC, Ebihara L (2002). "Functional role of the carboxyl terminal domain of human connexin 50 in gap junctional channels.". J. Membr. Biol. 186 (2): 101–12. doi:10.1007/s00232-001-0139-5. PMC 2744361. PMID 11944087.
Nielsen PA, Baruch A, Shestopalov VI; et al. (2004). "Lens connexins alpha3Cx46 and alpha8Cx50 interact with zonula occludens protein-1 (ZO-1).". Mol. Biol. Cell 14 (6): 2470–81. doi:10.1091/mbc.E02-10-0637. PMC 194895. PMID 12808044.
Arora A, Minogue PJ, Liu X; et al. (2006). "A novel GJA8 mutation is associated with autosomal dominant lamellar pulverulent cataract: further evidence for gap junction dysfunction in human cataract.". J. Med. Genet. 43 (1): e2. doi:10.1136/jmg.2005.034108. PMC 2564510. PMID 16397066.
Devi RR, Vijayalakshmi P (2006). "Novel mutations in GJA8 associated with autosomal dominant congenital cataract and microcornea.". Mol. Vis. 12: 190–5. PMID 16604058.
Zhang X, Zou T, Liu Y, Qi Y (2006). "The gating effect of calmodulin and calcium on the connexin50 hemichannel.". Biol. Chem. 387 (5): 595–601. doi:10.1515/BC.2006.076. PMID 16740131.
Ni X, Valente J, Azevedo MH; et al. (2007). "Connexin 50 gene on human chromosome 1q21 is associated with schizophrenia in matched case control and family-based studies.". J. Med. Genet. 44 (8): 532–6. doi:10.1136/jmg.2006.047944. PMC 2597930. PMID 17412882.
Kotsias BA, Salim M, Peracchia LL, Peracchia C (2007). "Interplay between cystic fibrosis transmembrane regulator and gap junction channels made of connexins 45, 40, 32 and 50 expressed in oocytes.". J. Membr. Biol. 214 (1): 1–8. doi:10.1007/s00232-006-0064-8. PMID 17546509.
Hansen L, Yao W, Eiberg H; et al. (2007). "Genetic heterogeneity in microcornea-cataract: five novel mutations in CRYAA, CRYGD, and GJA8.". Invest. Ophthalmol. Vis. Sci. 48 (9): 3937–44. doi:10.1167/iovs.07-0013. PMID 17724170.

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

Voltage-gated	L-type/Ca_vα 1.1 1.2 1.3 1.4 N-type/Ca_vα2.2 P-type/Ca_vα 2.1 Q-type/Ca_vα2.1 R-type/Ca_vα2.3 T-type/Ca_vα 3.1 3.2 3.3 α₂δ-subunits 1 2 β-subunits β1 β2 β3 β4 γ-subunits γ1 γ2 γ3 γ4 Cation channels of sperm 1 2 3 4 Two-pore channel 1 2

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel α β γ δ

Proton-gated	Amiloride-sensitive cation channel 1 2 3 4

Voltage-gated	Na_vα 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Na_vβ 1 2 3 4

K⁺: Potassium channel

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 K_Ca 1.1 2.1 2.2 2.3 3.1 4.1 4.2 5.1

Inward-rectifier	K_ATP K_ir 1.1 2.1 2.2 2.3 2.4 2.6 GIRK/K_ir 3.1 3.2 3.3 3.4 K_ir 4.1 4.2 5.1 6.1 6.2 7.1

Tandem pore domain	K2P 1 2 3 4 5 6 7 9 10 12 13 15 16 17 18

Voltage-gated	K_vα1-6 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 2.1 2.2 3.1 3.2 3.3 3.4 4.1 4.2 4.3 5.1 6.1 6.2 6.3 6.4 K_vα7-12 7.1 7.2 7.3 7.4 7.5 8.1 8.2 9.1 9.2 9.3 10.1 10.2 11.1/hERG 11.2 11.3 12.1 12.2 12.3 K_vβ 1 2 3 KCNIP 1 2 3 4 minK/ISK minK/ISK-like MiRP 1 2 3 Shaker gene

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

M⁺: TRP cation channel	TRPA (1) TRPC 1 2 3 4 4AP 5 6 7 TRPM 1 2 3 4 5 6 7 8 TRPML 1 2 3 TRPN TRPP 1 2 TRPV 1 2 3 4 5 6

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: Gap junction	Connexin: A GJA1 GJA3 GJA4 GJA5 GJA8 GJA9 GJA10 B GJB1 GJB2 GJB3 GJB4 GJB5 GJB6 GJB7 C GJC1 GJC2 GJC3 D GJD2 GJD3 GJD4) Innexin

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

This article is issued from Wikipedia - version of the Tuesday, October 06, 2015. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

GJA8

Related gene problems

Interactions

References

Further reading