CLDN14

CLDN14
Identifiers
Aliases	CLDN14 , DFNB29, claudin 14
External IDs	OMIM: 605608 MGI: 1860425 HomoloGene: 8115 GeneCards: CLDN14
Gene location (Human)
Chr.	Chromosome 21 (human)
End	36,576,569 bp
Gene location (Mouse)
Chr.	Chromosome 16 (mouse)
End	93,809,696 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; kidney; ; kidney tubule; ; body of pancreas; ; renal medulla; ; gallbladder; ; lower lobe of lung; ; appendix; ; right coronary artery; ; islet of Langerhans;
	Top expressed in
	hepatobiliary system; ; liver; ; left lobe of liver; ; hair follicle; ; parasympathetic nervous system; ; thyroid gland; ; secondary oocyte; ; sciatic nerve; ; pharynx; ; tongue;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	structural molecule activity ; identical protein binding ;
Cellular component	integral component of membrane ; cell junction ; plasma membrane ; endoplasmic reticulum ; membrane ; bicellular tight junction ;
Biological process	calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules ; protein-containing complex assembly ;
	Sources:Amigo / QuickGO
Orthologs
	23562
	56173
	ENSG00000159261
	ENSMUSG00000047109
	O95500
	Q9Z0S3
	NM_001146077 ; NM_001146078 ; NM_001146079 ; NM_012130 ; NM_144492 Contents See also ; References ; External links ; Further reading ;
	NM_001165925 ; NM_001165926 ; NM_019500
	NP_001139549 ; NP_001139550 ; NP_001139551 ; NP_036262 ; NP_652763
	NP_001159397 ; NP_001159398 ; NP_062373
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 25, 2024

Claudin-14 is a protein that in humans is encoded by the CLDN14 gene.^[5]^[6] It belongs to a related family of proteins called claudins.

The protein encoded by CLDN14 is an integral membrane protein and a component of tight junctions, one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets. Tight junctions form continuous seals around cells and serve 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 protein strands in the outer surface of the cell membrane, with complementary grooves in the inwardly facing extracytoplasmic leaflet. The CLDN14 protein also binds to WW domain of Yes-associated protein.

Defects in CLDN14 are the cause of an autosomal recessive form of nonsyndromic sensorineural deafness. Two transcript variants encoding the same protein have been found for this gene.^[6]

There are also suggestions that CLDN14 plays a role in tumour angiogenesis (blood vessel formation),^[7] as deletion of a single copy of this gene leads to tight junction defects and leaky blood vessels in a mouse model.

Polymorphisms in CLDN14 are associated with kidney stone risk. It is likely that additional roles for claudins in the pathogenesis of other types of kidney diseases have yet to be uncovered.

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-2 is a protein that in humans is encoded by the CLDN2 gene. It belongs to the group of claudins.

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-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: ENSG00000159261 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047109 - 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.
↑ Wilcox ER, Burton QL, Naz S, Riazuddin S, Smith TN, Ploplis B, Belyantseva I, Ben-Yosef T, Liburd NA, Morell RJ, Kachar B, Wu DK, Griffith AJ, Riazuddin S, Friedman TB (Feb 2001). "Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29". Cell. 104 (1): 165–72. doi: 10.1016/S0092-8674(01)00200-8 . PMID 11163249. S2CID 6346705.
1 2 "Entrez Gene: CLDN14 claudin 14".
↑ Baker M, Reynolds LE, Robinson SD, Lees DM, Parsons M, Elia G, et al. (2013). "Stromal Claudin14-Heterozygosity, but Not Deletion, Increases Tumour Blood Leakage without Affecting Tumour Growth". PLOS ONE. 8 (5): e62516. Bibcode:2013PLoSO...862516B. doi: 10.1371/journal.pone.0062516 . PMC 3652830 . PMID 23675413.

External links

Human CLDN14 genome location and CLDN14 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. S2CID 12132159.
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.
Chen HI, Sudol M (1995). "The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7819–23. Bibcode:1995PNAS...92.7819C. doi: 10.1073/pnas.92.17.7819 . PMC 41237 . PMID 7644498.
Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21". Nature. 405 (6784): 311–9. Bibcode:2000Natur.405..311H. doi: 10.1038/35012518 . PMID 10830953.
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.
Uyguner O, Emiroglu M, Uzumcu A, et al. (2004). "Frequencies of gap- and tight-junction mutations in Turkish families with autosomal-recessive non-syndromic hearing loss". Clin. Genet. 64 (1): 65–9. doi:10.1034/j.1399-0004.2003.00101.x. PMID 12791041. S2CID 29823828.
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.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Van Itallie CM, Gambling TM, Carson JL, Anderson JM (2005). "Palmitoylation of claudins is required for efficient tight-junction localization". J. Cell Sci. 118 (Pt 7): 1427–36. doi: 10.1242/jcs.01735 . PMID 15769849.
Wattenhofer M, Reymond A, Falciola V, et al. (2006). "Different mechanisms preclude mutant CLDN14 proteins from forming tight junctions in vitro". Hum. Mutat. 25 (6): 543–9. doi: 10.1002/humu.20172 . PMID 15880785. S2CID 27476200.
Hu YH, Warnatz HJ, Vanhecke D, et al. (2006). "Cell array-based intracellular localization screening reveals novel functional features of human chromosome 21 proteins". BMC Genomics. 7: 155. doi: 10.1186/1471-2164-7-155 . PMC 1526728 . PMID 16780588.
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.

Sticky cells, blood vessels and cancer – the paradox of Claudin-14 - Marianne Baker, Cancer Research UK Science Update blog, 14 June 2013

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000159261 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047109 - 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.

[pmid11163249-5] Wilcox ER, Burton QL, Naz S, Riazuddin S, Smith TN, Ploplis B, Belyantseva I, Ben-Yosef T, Liburd NA, Morell RJ, Kachar B, Wu DK, Griffith AJ, Riazuddin S, Friedman TB (Feb 2001). "Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29". Cell. 104 (1): 165–72. doi: 10.1016/S0092-8674(01)00200-8 . PMID 11163249. S2CID 6346705.

[entrez-6] 1 2 "Entrez Gene: CLDN14 claudin 14".

[pmid23675413-7] Baker M, Reynolds LE, Robinson SD, Lees DM, Parsons M, Elia G, et al. (2013). "Stromal Claudin14-Heterozygosity, but Not Deletion, Increases Tumour Blood Leakage without Affecting Tumour Growth". PLOS ONE. 8 (5): e62516. Bibcode:2013PLoSO...862516B. doi: 10.1371/journal.pone.0062516 . PMC 3652830 . PMID 23675413.

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CLDN14

Contents

See also

Related Research Articles

References

External links

Further reading