CLDN2

CLDN2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4YYX
Identifiers
Aliases	CLDN2 , claudin 2, OAZON
External IDs	OMIM: 300520 MGI: 1276110 HomoloGene: 9621 GeneCards: CLDN2
Gene location (Human)
Chr.	X chromosome (human)
End	106,930,861 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	138,712,135 bp
RNA expression pattern
	Top expressed in
	pancreatic ductal cell; ; gallbladder; ; islet of Langerhans; ; kidney; ; right lobe of liver; ; seminal vesicula; ; renal cortex; ; renal medulla; ; duodenum; ; caput epididymis;
	Top expressed in
	kidney; ; proximal tubule; ; crypt of lieberkuhn of small intestine; ; left colon; ; yolk sac; ; left lobe of liver; ; duodenum; ; ciliary body; ; ileum; ; retinal pigment epithelium;
	More reference expression data
	n/a
Gene ontology
Molecular function	protein binding ; identical protein binding ; structural molecule activity ;
Cellular component	cell junction ; integral component of membrane ; bicellular tight junction ; plasma membrane ; membrane ;
Biological process	calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules ;
	Sources:Amigo / QuickGO
Orthologs
	9075
	12738
	ENSG00000165376
	ENSMUSG00000047230
	P57739
	O88552
	NM_020384 ; NM_001171092 ; NM_001171095
	NM_016675
	NP_001164563 ; NP_001164566 ; NP_065117
	NP_057884
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated November 29, 2023

Claudin-2 is a protein that in humans is encoded by the CLDN2 gene.^[5]^[6] It belongs to the group of claudins.

Function

Claudin-2 is expressed in cation-leaky epithelia such as that of the kidney proximal tubule.^[7] Mice that are deficient in claudin-2 have reduced reabsorption of Na ⁺ in the proximal tubule, consistent with a role in paracellular transport. Similar results have been obtained with cultured cells, as overexpression in claudin-2 lacking cells leads to increase of permeability for small cations.^[8] Furthermore, claudin-2 has been shown to form paracellular channels for water.^[9]

Related Research Articles

Claudins are a family of proteins which, along with occludin, are the most important components of the tight junctions. Tight junctions establish the paracellular barrier that controls the flow of molecules in the intercellular space between the cells of an epithelium. They have four transmembrane domains, with the N-terminus and the C-terminus in the cytoplasm.

<span class="mw-page-title-main">Occludin</span> Mammalian protein found in Homo sapiens

Occludin is a transmembrane protein that regulates the permeability of epithelial and endothelial barriers. It was first identified in epithelial cells as a 65 kDa integral plasma-membrane protein localized at the tight junctions. Together with Claudins, and zonula occludens-1 (ZO-1), occludin has been considered a staple of tight junctions, and although it was shown to regulate the formation, maintenance, and function of tight junctions, its precise mechanism of action remained elusive and most of its actions were initially attributed to conformational changes following selective phosphorylation, and its redox-sensitive dimerization. However, mounting evidence demonstrated that occludin is not only present in epithelial/endothelial cells, but is also expressed in large quantities in cells that do not have tight junctions but have very active metabolism: pericytes, neurons and astrocytes, oligodendrocytes, dendritic cells, monocytes/macrophages lymphocytes, and myocardium. Recent work, using molecular modeling, supported by biochemical and live-cell experiments in human cells demonstrated that occludin is a NADH oxidase that influences critical aspects of cell metabolism like glucose uptake, ATP production and gene expression. Furthermore, manipulation of occludin content in human cells is capable of influencing the expression of glucose transporters, and the activation of transcription factors like NFkB, and histone deacetylases like sirtuins, which proved capable of diminishing HIV replication rates in infected human macrophages under laboratory conditions.

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

Claudin 4, also known as CLDN4, is a protein which in humans is encoded by the CLDN4 gene. It belongs to the group of claudins.

Claudin-5 is a protein that in humans is encoded by the CLDN5 gene. It belongs to the group of claudins.

Claudin 3, also known as CLDN3, is a protein which in humans is encoded by the CLDN3 gene. It is a member of the claudin protein family.

Claudin-7 is a protein that in humans is encoded by the CLDN7 gene. It belongs to the group of claudins.

Claudin-6 is a protein that in humans is encoded by the CLDN6 gene. It belongs to the group of claudins. The knockout mice of mouse homolog exhibit no phenotype, indicating that claudin-6 is dispensable for normal development and homeostasis.

Claudin-12 is a protein that in humans is encoded by the CLDN12 gene. It belongs to the group of claudins.

Claudin-8 is a protein that in humans is encoded by the CLDN8 gene. It belongs to the group of claudins.

Claudin-16 is a protein that in humans is encoded by the CLDN16 gene. It belongs to the group of claudins.

Claudin-14 is a protein that in humans is encoded by the CLDN14 gene. It belongs to a related family of proteins called claudins.

Claudin-9 is a protein that in humans is encoded by the CLDN9 gene. It belongs to the group of claudins.

Claudin-17 is a protein that in humans is encoded by the CLDN17 gene. It belongs to the group of claudins; claudins are cell-cell junction proteins that keep that maintains cell- and tissue-barrier function. It forms anion-selective paracellular channels and is localized mainly in kidney proximal tubules.

Claudin-10 is a protein that in humans is encoded by the CLDN10 gene. It belongs to the group of claudins.

Claudin-15 is a protein that in humans is encoded by the CLDN15 gene. It belongs to the group of claudins. Among its related pathways are Blood-Brain Barrier and Immune Cell Transmigration: VCAM-1/CD106 Signaling Pathways and Tight junction. GO annotations related to this gene include identical protein binding and structural molecule activity. An important paralog of this gene is CLDN10.

Claudin-19 is a protein that in humans is encoded by the CLDN19 gene. It belongs to the group of claudins. Claudin-19 has been implicated in magnesium transport.

Claudin-20 is a protein that in humans is encoded by the CLDN20 gene. It belongs to the group of claudins.

Claudin-18 is a protein that in humans is encoded by the CLDN18 gene. It belongs to the group of claudins.

Claudin-22 is a protein that in humans is encoded by the CLDN22 gene. It belongs to the group of claudins.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000165376 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047230 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Morita K, Furuse M, Fujimoto K, Tsukita S (March 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. Bibcode:1999PNAS...96..511M. doi: 10.1073/pnas.96.2.511 . PMC 15167 . PMID 9892664.
1 2 "Entrez Gene: CLDN2 claudin 2".
↑ Muto, S.; Hata, M.; Taniguchi, J.; Tsuruoka, S.; Moriwaki, K.; Saitou, M.; Furuse, K.; Sasaki, H.; Fujimura, A.; Imai, M.; Kusano, E.; Tsukita, S.; Furuse, M. (2010). "Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules". Proceedings of the National Academy of Sciences. 107 (17): 8011–8016. Bibcode:2010PNAS..107.8011M. doi: 10.1073/pnas.0912901107 . PMC 2867900 . PMID 20385797.
↑ Amasheh, S; Meiri, N; Gitter, A. H.; Schöneberg, T; Mankertz, J; Schulzke, J. D.; Fromm, M (2002). "Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells". Journal of Cell Science. 115 (Pt 24): 4969–76. doi:10.1242/jcs.00165. PMID 12432083.
↑ Rosenthal, R.; Milatz, S.; Krug, S. M.; Oelrich, B.; Schulzke, J. -D.; Amasheh, S.; Gunzel, D.; Fromm, M. (2010). "Claudin-2, a component of the tight junction, forms a paracellular water channel". Journal of Cell Science. 123 (11): 1913–1921. doi:10.1242/jcs.060665. PMID 20460438.

External links

Human CLDN2 genome location and CLDN2 gene details page in the UCSC Genome Browser .

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. S2CID 26473781.
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. S2CID 36524601.
Tsukita S, Furuse M (2003). "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.
Furuse M, Fujita K, Hiiragi T, et al. (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.
Itoh M, Furuse M, Morita K, et al. (2000). "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.
Sakaguchi T, Gu X, Golden HM, et al. (2002). "Cloning of the human claudin-2 5'-flanking region revealed a TATA-less promoter with conserved binding sites in mouse and human for caudal-related homeodomain proteins and hepatocyte nuclear factor-1alpha". J. Biol. Chem. 277 (24): 21361–70. doi: 10.1074/jbc.M110261200 . PMID 11934881.
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.
Colegio OR, Van Itallie C, Rahner C, Anderson JM (2003). "Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture". Am. J. Physiol., Cell Physiol. 284 (6): C1346–54. doi:10.1152/ajpcell.00547.2002. PMID 12700140.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697 . PMID 12975309.
Mankertz J, Hillenbrand B, Tavalali S, et al. (2004). "Functional crosstalk between Wnt signaling and Cdx-related transcriptional activation in the regulation of the claudin-2 promoter activity". Biochem. Biophys. Res. Commun. 314 (4): 1001–7. doi:10.1016/j.bbrc.2003.12.185. PMID 14751232.
Yamauchi K, Rai T, Kobayashi K, et al. (2004). "Disease-causing mutant WNK4 increases paracellular chloride permeability and phosphorylates claudins". Proc. Natl. Acad. Sci. U.S.A. 101 (13): 4690–4. Bibcode:2004PNAS..101.4690Y. doi: 10.1073/pnas.0306924101 . PMC 384808 . PMID 15070779.
Escaffit F, Boudreau F, Beaulieu JF (2005). "Differential expression of claudin-2 along the human intestine: Implication of GATA-4 in the maintenance of claudin-2 in differentiating cells". J. Cell. Physiol. 203 (1): 15–26. doi:10.1002/jcp.20189. PMID 15389642. S2CID 39780124.
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. 15 (2): 339–359. doi:10.1021/acs.jproteome.5b00769. PMC 4777318 . PMID 26680015.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000165376 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047230 - 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.

[pmid9892664-5] Morita K, Furuse M, Fujimoto K, Tsukita S (March 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. Bibcode:1999PNAS...96..511M. doi: 10.1073/pnas.96.2.511 . PMC 15167 . PMID 9892664.

[entrez-6] 1 2 "Entrez Gene: CLDN2 claudin 2".

[7] Muto, S.; Hata, M.; Taniguchi, J.; Tsuruoka, S.; Moriwaki, K.; Saitou, M.; Furuse, K.; Sasaki, H.; Fujimura, A.; Imai, M.; Kusano, E.; Tsukita, S.; Furuse, M. (2010). "Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules". Proceedings of the National Academy of Sciences. 107 (17): 8011–8016. Bibcode:2010PNAS..107.8011M. doi: 10.1073/pnas.0912901107 . PMC 2867900 . PMID 20385797.

[8] Amasheh, S; Meiri, N; Gitter, A. H.; Schöneberg, T; Mankertz, J; Schulzke, J. D.; Fromm, M (2002). "Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells". Journal of Cell Science. 115 (Pt 24): 4969–76. doi:10.1242/jcs.00165. PMID 12432083.

[9] Rosenthal, R.; Milatz, S.; Krug, S. M.; Oelrich, B.; Schulzke, J. -D.; Amasheh, S.; Gunzel, D.; Fromm, M. (2010). "Claudin-2, a component of the tight junction, forms a paracellular water channel". Journal of Cell Science. 123 (11): 1913–1921. doi:10.1242/jcs.060665. PMID 20460438.

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CLDN2

Contents

Function

Related Research Articles

References

External links

Further reading