Biology:Tight junction protein 1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Zonula occludens-1 ZO-1, also known as Tight junction protein-1 is a 220-kD peripheral membrane protein that is encoded by the TJP1 gene in humans.[1] It belongs to the family of zonula occludens proteins (ZO-1, ZO-2, and ZO-3), which are tight junction-associated proteins and of which, ZO-1 is the first to be cloned. It was first isolated in 1986 by Stevenson and Goodenough using a monoclonal antibody raised in rodent liver to recognise a 225-kD polypeptide in whole liver homogenates and in tight junction-enriched membrane fractions.[2] It has a role as a scaffold protein which cross-links and anchors Tight Junction (TJ) strand proteins, which are fibril-like structures within the lipid bilayer, to the actin cytoskeleton.[3]

Function

This gene encodes a protein located on a cytoplasmic membrane surface of intercellular tight junctions. The encoded protein may be involved in signal transduction at cell–cell junctions. Two transcript variants encoding distinct isoforms have been identified for this gene.[4]

Interactions

Tight junction protein 1 has been shown to interact with:


See also

References

  1. ↑ "Localization of the tight junction protein gene TJP1 to human chromosome 15q13, distal to the Prader-Willi/Angelman region, and to mouse chromosome 7". Genomics 30 (3): 594–7. December 1995. doi:10.1006/geno.1995.1281. PMID 8825647. 
  2. ↑ "Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia". The Journal of Cell Biology 103 (3): 755–66. September 1986. doi:10.1083/jcb.103.3.755. PMID 3528172. 
  3. ↑ "Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments". The Journal of Cell Biology 138 (1): 181–92. July 1997. doi:10.1083/jcb.138.1.181. PMID 9214391. 
  4. ↑ "Entrez Gene: TJP1 tight junction protein 1 (zona occludens 1)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7082. 
  5. ↑ "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry 275 (36): 27979–88. Sep 2000. doi:10.1074/jbc.M002363200. PMID 10856295. 
  6. ↑ "The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity". Journal of Cell Science 116 (Pt 19): 3879–91. Oct 2003. doi:10.1242/jcs.00704. PMID 12953056. https://archive-ouverte.unige.ch/unige:11233/ATTACHMENT01. 
  7. ↑ 7.0 7.1 "Lens connexins alpha3Cx46 and alpha8Cx50 interact with zonula occludens protein-1 (ZO-1)". Molecular Biology of the Cell 14 (6): 2470–81. Jun 2003. doi:10.1091/mbc.E02-10-0637. PMID 12808044. 
  8. ↑ "The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein". Current Biology 8 (16): 931–4. 1998. doi:10.1016/S0960-9822(07)00375-2. PMID 9707407. 
  9. ↑ "Neph1 and nephrin interaction in the slit diaphragm is an important determinant of glomerular permeability". The Journal of Clinical Investigation 112 (2): 209–21. Jul 2003. doi:10.1172/JCI18242. PMID 12865409. 
  10. ↑ "The carboxyl terminus of Neph family members binds to the PDZ domain protein zonula occludens-1". The Journal of Biological Chemistry 278 (15): 13417–21. Apr 2003. doi:10.1074/jbc.C200678200. PMID 12578837. 
  11. ↑ "In vivo interaction of AF-6 with activated Ras and ZO-1". Biochemical and Biophysical Research Communications 259 (1): 103–7. May 1999. doi:10.1006/bbrc.1999.0731. PMID 10334923. 
  12. ↑ 12.0 12.1 "The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton". The Journal of Biological Chemistry 273 (45): 29745–53. Nov 1998. doi:10.1074/jbc.273.45.29745. PMID 9792688. 
  13. ↑ "Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress". The Biochemical Journal 368 (Pt 2): 471–81. Dec 2002. doi:10.1042/BJ20011804. PMID 12169098. 
  14. ↑ 14.0 14.1 "Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3". The Journal of Biological Chemistry 274 (49): 35179–85. Dec 1999. doi:10.1074/jbc.274.49.35179. PMID 10575001. 
  15. ↑ "Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin". The Journal of Biological Chemistry 274 (9): 5981–6. Feb 1999. doi:10.1074/jbc.274.9.5981. PMID 10026224. 

Further reading

External links

  • Overview of all the structural information available in the PDB for UniProt: Q07157 (Human Tight junction protein ZO-1) at the PDBe-KB.
  • Overview of all the structural information available in the PDB for UniProt: P39447 (Mouse Tight junction protein ZO-1) at the PDBe-KB.




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