Tight junction protein 1

Last updated
Protein TJP1 PDB 2h2b.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases TJP1 , ZO-1, Tight junction protein 1
External IDs OMIM: 601009 MGI: 98759 HomoloGene: 2445 GeneCards: TJP1
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC) Chr 15: 29.7 – 29.97 Mb Chr 7: 64.95 – 65.18 Mb
PubMed search [3] [4]
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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. [5] 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. [6] 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. [7]


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. [8]


Tight junction protein 1 has been shown to interact with:

See also

Related Research Articles

<span class="mw-page-title-main">Tight junction</span> Structure preventing inter-cell leakage

Tight junctions, also known as occluding junctions or zonulae occludentes, are multiprotein junctional complexes whose canonical function is to prevent leakage of solutes and water and seals between the epithelial cells. They also play a critical role maintaining the structure and permeability of endothelial cells. Tight junctions may also serve as leaky pathways by forming selective channels for small cations, anions, or water. The corresponding junctions that occur in invertebrates are septate junctions.

<span class="mw-page-title-main">Adherens junction</span>

Adherens junctions are protein complexes that occur at cell–cell junctions, cell–matrix junctions in epithelial and endothelial tissues, usually more basal than tight junctions. An adherens junction is defined as a cell junction whose cytoplasmic face is linked to the actin cytoskeleton. They can appear as bands encircling the cell or as spots of attachment to the extracellular matrix . Adherens junctions uniquely disassemble in uterine epithelial cells to allow the blastocyst to penetrate between epithelial cells.

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

Occludin is an enzyme that oxidizes NADH. 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.

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

Plakoglobin, also known as junction plakoglobin or gamma-catenin, is a protein that in humans is encoded by the JUP gene. Plakoglobin is a member of the catenin protein family and homologous to β-catenin. Plakoglobin is a cytoplasmic component of desmosomes and adherens junctions structures located within intercalated discs of cardiac muscle that function to anchor sarcomeres and join adjacent cells in cardiac muscle. Mutations in plakoglobin are associated with arrhythmogenic right ventricular dysplasia.

<span class="mw-page-title-main">Alpha catenin</span> Primary protein link between cadherins and the actin cytoskeleton

Alpha-catenin functions as the primary protein link between cadherins and the actin cytoskeleton. It has been reported that the actin binding proteins vinculin and alpha-actinin can bind to alpha-catenin. It has been suggested that alpha-catenin does not bind with high affinity to both actin filaments and the E-cadherin-beta-catenin complex at the same time. It has been observed that when alpha-catenin is not in a molecular complex with beta-catenin, it dimerizes and functions to regulate actin filament assembly, possibly by competing with Arp2/3 protein. Alpha catenin exhibits significant protein dynamics. However, a protein complex including a cadherin, actin, beta-catenin and alpha-catenin has not been isolated.

<span class="mw-page-title-main">Afadin</span> Protein-coding gene in the species Homo sapiens

Afadin is a protein that in humans is encoded by the AFDN gene.

<span class="mw-page-title-main">CLDN1</span>

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

<span class="mw-page-title-main">Tight junction protein 2</span> Protein found in humans

Tight junction protein ZO-2 is a protein that in humans is encoded by the TJP2 gene.

<span class="mw-page-title-main">CLDN4</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">IQGAP1</span>

Ras GTPase-activating-like protein IQGAP1 (IQGAP1) also known as p195 is a ubiquitously expressed protein that in humans is encoded by the IQGAP1 gene. IQGAP1 is a scaffold protein involved in regulating various cellular processes ranging from organization of the actin cytoskeleton, transcription, and cellular adhesion to regulating the cell cycle.

<span class="mw-page-title-main">F11 receptor</span>

Junctional adhesion molecule A is a protein that in humans is encoded by the F11R gene. It has also been designated as CD321.

<span class="mw-page-title-main">CLDN5</span>

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

<span class="mw-page-title-main">CLDN3</span>

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.

<span class="mw-page-title-main">CLDN2</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">InaD-like protein</span> Protein-coding gene in the species Homo sapiens

InaD-like protein is a protein that in humans is encoded by the PATJ gene.

<span class="mw-page-title-main">Cingulin</span> Protein-coding gene in the species Homo sapiens

Cingulin is a cytosolic protein encoded by the CGN gene in humans localized at tight junctions (TJs) of vertebrate epithelial and endothelial cells.

<span class="mw-page-title-main">Stress fiber</span> Contractile actin bundles found in non-muscle cells

Stress fibers are contractile actin bundles found in non-muscle cells. They are composed of actin (microfilaments) and non-muscle myosin II (NMMII), and also contain various crosslinking proteins, such as α-actinin, to form a highly regulated actomyosin structure within non-muscle cells. Stress fibers have been shown to play an important role in cellular contractility, providing force for a number of functions such as cell adhesion, migration and morphogenesis.

<span class="mw-page-title-main">Catenin alpha-1</span> Protein-coding gene in the species Homo sapiens

αE-catenin, also known as Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. αE-catenin is highly expressed in cardiac muscle and localizes to adherens junctions at intercalated disc structures where it functions to mediate the anchorage of actin filaments to the sarcolemma. αE-catenin also plays a role in tumor metastasis and skin cell function.

<span class="mw-page-title-main">TJP3</span> Protein-coding gene in the species Homo sapiens

Tight junction protein ZO-3 is a protein that in humans is encoded by the TJP3 gene.

<span class="mw-page-title-main">Cingulin-like protein 1</span>

Cingulin-like protein 1, also known as paracingulin or junction-associated-coiled-coil protein (JACOP), is a protein which is encoded by the CGNL1 gene.


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Further reading