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FLASH GENE
Symbol TJP1 contributors: mct/npt/pgu - updated : 15-06-2016
HGNC name tight junction protein 1 (zona occludens 1)
HGNC id 11827
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N terminal (MAGUK-like),three Dlg,(DHR/GLGZ/PDZ) motifs, which are necessary for its function and playing a central role in assembling diverse protein complexes through their ability to recognize short peptide motifs on other proteins (PDZ2 domain binding to GJA1)
  • a SH3 domain
  • a unique proline-rich region cosedimenting with F-actin (ABR,
  • actin-binding region), a 220-AAs domain within the C-terminal half, mediating association with actin, at least in part
    HOMOLOGY
    interspecies homolog to yeast guanylate kinase
    homolog to Drosophila lethal discs large tumor suppressor protein
    Homologene
    FAMILY
  • MAGUK (membrane-associated guanylate kinase homolog) family
  • CATEGORY adhesion , chaperone/stress , structural protein
    SUBCELLULAR LOCALIZATION     plasma membrane,junction,tight
        intracellular
    intracellular,cytoplasm,cytosolic
    intracellular,nucleus
    text
  • co-localized with JAM3 to adherens-like junctions
  • glomeruli predominantly to points where the slit diaphragm is inserted into the lateral cell membrane of the foot process
  • SYMPK co-localized with TJP1 at tight junctions
  • basic FUNCTION
  • F actin filament binding scaffold protein
  • structural component of tight junction and adherens junction
  • SHROOM2 and TJP1 form a tight-junction-associated scaffolding complex, possibly linked to myosin VIIa, that bridges the junctional membrane to the underlying cytoskeleton, thereby contributing to the stabilization of these junctions
  • colocalised in the salivary excretory ducts with CLDN16 and occludin suggesting a potential role in paracellular calcium and magnesium transport
  • central player in the control of gap junction (GJ) dynamics
  • regulates GJA1-mediated gap junctional communication in osteoblastic cells and alters the membrane localization of GJA1
  • essential for cytoskeletally-mediated barrier regulation
  • TJP1 and PLEKHA7 are paracingulin-interacting proteins that are involved in its recruitment to epithelial tight and adherens junctions, respectively
  • is a response protein to inner medullary tonicity and extracellular stressors can promote TJP1 protein expression, tyrosine phosphorylation and cytoskeleton association
  • TJP1 and TJP2 are required not only for TJ assembly but also for regulating the organization and functional activity of the apical cytoskeleton, particularly the perijunctional actomyosin ring
  • CPEB1-mediated TJP1 mRNA localization is essential for tight-junction assembly and mammary epithelial cell polarity
  • VCL and TJP1 anchor the actin cytoskeleton to the sarcolemma
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • ABCB1 and an integrated component of the occludin/zonula occludens 1 (TJP1) adhesion complex at the BTB, structurally interacted with PTK2, creating the OCLN/TJP1/PTK2/ABCB1 regulatory complex
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • binding directly to the C terminus of claudins
  • binding to occludin and alpha catenin
  • associating with F-actin (playing a role in several different steps of junction assembly)
  • bind to the C-terminus of OCLN
  • interaction with OCLN and PTPRJ specific (OCLN and TJP1 were dephosphorylated by PTPRJ but not the other phosphatases)
  • targets to gap junction edges independently of several known PDZ2-mediated interactions, including TJP1 homodimerization, heterodimerization with TJP2, and direct TJP1 binding to the C-terminal residues of GJA1) (H
  • by interacting with GJA1, plays a role in the down-regulation and decreased size of GJA1 gap junctions in congestive heart failure
  • interacting with KIRREL (tyrosine phosphorylation of KIRREL results in significantly increased KIRREL and TJP1 binding, suggesting a critical role for KIRREL tyrosine phosphorylation in reorganizing the KIRREL-TJP1 complex)
  • interacting with MYLK (MYLK activity is critical to TJP1, but not claudin-1, occludin, or actin) exchange at the tight junction)
  • interaction between TAZ and TJP1, TJP2, through TAZ C-terminal PDZ binding motif
  • TJP1 and the adherens junction protein PLEKHA7 as paracingulin-binding proteins
  • GJA8 requires an intact PDZ-binding motif and TJP1 for the formation of functional intercellular channels
  • interaction with UBN1 (N-terminal domains of the UBN1 and TJP1 proteins triggered a functional interaction inside the cell)
  • ARHGEF11 associates with tight junctions (TJs) by binding to TJP1, in polarized epithelial cells
  • KLF4 regulates blood-tumor barrier permeability via TJP1, OCLN and CLDN5
  • direct interaction between VCL and TJP1, illustrating how VCL plays a crucial role in stabilizing gap junctions and myocyte integrity
  • CALCR interacts with zonula occludens 1 (TJP1) through PDZ interaction to destabilize tight junctions and increase invasion of prostate cancers (PCs) cells
  • cell & other
    REGULATION
    Other upregulated, phosphorylated and linked to the actin cytoskeleton in response to hypertonic stress (
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --low  
    in patients with heart failure, with diminished expression levels of GJA1, suggesting that TJP1 plays an important role in gap junction formation and gap junction plaque stability
    constitutional     --other  
    present in apical tight junctions in normal epithelium but were dislocated to the basolateral position in patients with inactive Crohn disease (
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    cancer  
    networking between TAZ and TJP1 and TJP2 offers a promising target in the control of proliferation and apoptosis, epithelial-mesenchymal transition and migration capacity of cancer cells
    cancerreproductiveprostate
    prevention of CALCR-TJP1 interaction abolishes calcitonin-induced invasion, and can serve as a novel therapeutic tool to treat aggressive prostate cancers
    ANIMAL & CELL MODELS