CLDN1

CLDN1
Identifiers
AliasesCLDN1, CLD1, ILVASC, SEMP1, claudin 1
External IDsMGI: 1276109 HomoloGene: 9620 GeneCards: CLDN1
Gene location (Human)
Chr.Chromosome 3 (human)[1]
Band3q28Start190,305,701 bp[1]
End190,322,475 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

9076

12737

Ensembl

ENSG00000163347

ENSMUSG00000022512

UniProt

O95832

O88551

RefSeq (mRNA)

NM_021101

NM_016674

RefSeq (protein)

NP_066924

NP_057883

Location (UCSC)Chr 3: 190.31 – 190.32 MbChr 16: 26.36 – 26.37 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Claudin-1 is a protein that in humans is encoded by the CLDN1 gene.[5][6] It belongs to the group of claudins.

Function

Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are composed of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet, with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this gene, a member of the claudin family, is an integral membrane protein and a component of tight junction strands. Loss of function mutations result in neonatal ichthyosis-sclerosing cholangitis syndrome.[7]

Interactions

CLDN1 has been shown to interact with CLDN5[8] and CLDN3.[8]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000163347 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022512 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Halford S, Spencer P, Greenwood J, Winton H, Hunt DM, Adamson P (Jun 2000). "Assignment of claudin-1 (CLDN1) to human chromosome 3q28-->q29 with somatic cell hybrids". Cytogenet. Cell Genet. 88 (3–4): 217. doi:10.1159/000015553. PMID 10828592.
  6. ↑ Morita K, Furuse M, Fujimoto K, Tsukita S (Mar 1999). "Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands". Proc. Natl. Acad. Sci. U.S.A. 96 (2): 511–6. doi:10.1073/pnas.96.2.511. PMC 15167. PMID 9892664.
  7. ↑ "Entrez Gene: CLDN1 claudin 1".
  8. 1 2 Coyne CB, Gambling TM, Boucher RC, Carson JL, Johnson LG (Nov 2003). "Role of claudin interactions in airway tight junctional permeability". Am. J. Physiol. Lung Cell Mol. Physiol. 285 (5): L1166–78. doi:10.1152/ajplung.00182.2003. PMID 12909588.

Further reading

  • Kniesel U, Wolburg H (2000). "Tight junctions of the blood-brain barrier". Cell. Mol. Neurobiol. 20 (1): 57–76. doi:10.1023/A:1006995910836. PMID 10690502.
  • Heiskala M, Peterson PA, Yang Y (2001). "The roles of claudin superfamily proteins in paracellular transport". Traffic. 2 (2): 93–8. doi:10.1034/j.1600-0854.2001.020203.x. PMID 11247307.
  • Tsukita S, Furuse M, Itoh M (2001). "Multifunctional strands in tight junctions". Nat. Rev. Mol. Cell Biol. 2 (4): 285–93. doi:10.1038/35067088. PMID 11283726.
  • Tsukita S, Furuse M (2002). "Claudin-based barrier in simple and stratified cellular sheets". Curr. Opin. Cell Biol. 14 (5): 531–6. doi:10.1016/S0955-0674(02)00362-9. PMID 12231346.
  • González-Mariscal L, Betanzos A, Nava P, Jaramillo BE (2003). "Tight junction proteins". Prog. Biophys. Mol. Biol. 81 (1): 1–44. doi:10.1016/S0079-6107(02)00037-8. PMID 12475568.
  • Swisshelm K, Macek R, Kubbies M (2005). "Role of claudins in tumorigenesis". Adv. Drug Deliv. Rev. 57 (6): 919–28. doi:10.1016/j.addr.2005.01.006. PMID 15820559.
  • King JE, Eugenin EA, Buckner CM, Berman JW (2006). "HIV tat and neurotoxicity". Microbes Infect. 8 (5): 1347–57. doi:10.1016/j.micinf.2005.11.014. PMID 16697675.
  • Ye J (2007). "Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus". PLoS Pathog. 3 (8): e108. doi:10.1371/journal.ppat.0030108. PMC 1959368. PMID 17784784.
  • Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita S (1998). "Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin". J. Cell Biol. 141 (7): 1539–50. doi:10.1083/jcb.141.7.1539. PMC 2132999. PMID 9647647.
  • Swisshelm K, Machl A, Planitzer S, Robertson R, Kubbies M, Hosier S (1999). "SEMP1, a senescence-associated cDNA isolated from human mammary epithelial cells, is a member of an epithelial membrane protein superfamily". Gene. 226 (2): 285–95. doi:10.1016/S0378-1119(98)00553-8. PMID 9931503.
  • Furuse M, Sasaki H, Tsukita S (1999). "Manner of interaction of heterogeneous claudin species within and between tight junction strands". J. Cell Biol. 147 (4): 891–903. doi:10.1083/jcb.147.4.891. PMC 2156154. PMID 10562289.
  • Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S (1999). "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins". J. Cell Biol. 147 (6): 1351–63. doi:10.1083/jcb.147.6.1351. PMC 2168087. PMID 10601346.
  • Krämer F, White K, Kubbies M, Swisshelm K, Weber BH (2000). "Genomic organization of claudin-1 and its assessment in hereditary and sporadic breast cancer". Hum. Genet. 107 (3): 249–56. doi:10.1007/s004390000375. PMID 11071387.
  • Miyamori H, Takino T, Kobayashi Y, Tokai H, Itoh Y, Seiki M, Sato H (2001). "Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases". J. Biol. Chem. 276 (30): 28204–11. doi:10.1074/jbc.M103083200. PMID 11382769.
  • Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S (2002). "Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule". J. Biol. Chem. 277 (1): 455–61. doi:10.1074/jbc.M109005200. PMID 11689568.
  • Liu F, Koval M, Ranganathan S, Fanayan S, Hancock WS, Lundberg EK, Beavis RC, Lane L, Duek P, McQuade L, Kelleher NL, Baker MS (2015). "A systems proteomics view of the endogenous human claudin protein family". J Proteome Res. doi:10.1021/acs.jproteome.5b00769. PMID 26680015.


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