CK2-dependent phosphorylation of occludin regulates the interaction with ZO-proteins and tight junction integrity.

scientific article published on 10 June 2013

CK2-dependent phosphorylation of occludin regulates the interaction with ZO-proteins and tight junction integrity. is …
instance of (P31):
scholarly articleQ13442814

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P6179Dimensions Publication ID1039189308
P356DOI10.1186/1478-811X-11-40
P932PMC publication ID3695765
P698PubMed publication ID23758859

P50authorMichael FrommQ30505679
Susanne M KrugQ47968279
Julie Katharina WestphalQ64762164
P2093author name stringIngolf E Blasig
Otmar Huber
Rudolf Tauber
Max J Dörfel
Jimmi Cording
Sonnhild Mittag
Christian Bellmann
P2860cites workTight junction-associated MARVEL proteins marveld3, tricellulin, and occludin have distinct but overlapping functionsQ24299926
Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cellsQ24310946
PKC eta regulates occludin phosphorylation and epithelial tight junction integrityQ24311692
Casein kinase I epsilon associates with and phosphorylates the tight junction protein occludinQ24317673
Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cellsQ24515257
Occludin: a novel integral membrane protein localizing at tight junctionsQ24657666
Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctionsQ24672971
Protein kinase C regulates the phosphorylation and cellular localization of occludinQ28212556
Tight junction proteinsQ28217124
Physiology and function of the tight junctionQ28270069
The occludin and ZO-1 complex, defined by small angle X-ray scattering and NMR, has implications for modulating tight junction permeabilityQ30010066
ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeletonQ30157199
Tricellulin forms a barrier to macromolecules in tricellular tight junctions without affecting ion permeabilityQ30491701
Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2.Q31146058
Bile acids modulate tight junction structure and barrier function of Caco-2 monolayers via EGFR activation.Q33317737
Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin.Q33874518
Epithelial barriers in homeostasis and diseaseQ34093056
Inhibition of glycogen synthase kinase 3β promotes tight junction stability in brain endothelial cells by half-life extension of occludin and claudin-5.Q34589682
Role of claudin species-specific dynamics in reconstitution and remodeling of the zonula occludensQ34888133
Occludin S408 phosphorylation regulates tight junction protein interactions and barrier functionQ34918139
Elucidating the principles of the molecular organization of heteropolymeric tight junction strands.Q35107926
Epithelial cell adhesion and the regulation of gene expressionQ35147365
Protein kinase CK2 in health and disease: CK2: a key player in cancer biologyQ35270830
"Targeted disruption of the epithelial-barrier by Helicobacter pylori".Q35576548
Occludin: structure, function and regulationQ36093750
Mammalian tight junctions in the regulation of epithelial differentiation and proliferationQ36228546
Tight Junction Pore and Leak Pathways: A Dynamic DuoQ36305755
Early embryonic lethality of mice lacking ZO-2, but Not ZO-3, reveals critical and nonredundant roles for individual zonula occludens proteins in mammalian developmentQ36483466
Deficiency of zonula occludens-1 causes embryonic lethal phenotype associated with defected yolk sac angiogenesis and apoptosis of embryonic cellsQ36678082
Crosstalk of tight junction components with signaling pathwaysQ36976365
Zona occludens-2 inhibits cyclin D1 expression and cell proliferation and exhibits changes in localization along the cell cycle.Q37078622
Cytokine regulation of tight junctionsQ37308566
Tight junction-based epithelial microenvironment and cell proliferationQ37333599
Occludin phosphorylation and ubiquitination regulate tight junction trafficking and vascular endothelial growth factor-induced permeabilityQ37344103
Tight junctions and the regulation of gene expressionQ37361719
Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: linking development and cancer.Q37456232
Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: a dynamic affair.Q37456242
Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survivalQ37456248
The dual role of zonula occludens (ZO) proteinsQ37708020
Occludin protein family: oxidative stress and reducing conditionsQ37828522
Modulation of tight junction structure and function by kinases and phosphatases targeting occludinQ37982360
Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayerQ38304743
Tricellulin forms homomeric and heteromeric tight junctional complexes.Q39730623
On the self-association potential of transmembrane tight junction proteins.Q40321024
Assembly of tight junction is regulated by the antagonism of conventional and novel protein kinase C isoformsQ40356717
Structure of the conserved cytoplasmic C-terminal domain of occludin: identification of the ZO-1 binding surfaceQ40388825
A second protein kinase CK1-mediated step negatively regulates Wnt signalling by disrupting the lymphocyte enhancer factor-1/beta-catenin complex.Q40450708
Establishment and characterization of cultured epithelial cells lacking expression of ZO-1.Q40528997
The specific fates of tight junction proteins in apoptotic epithelial cellsQ40571657
The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junctionQ40869408
Tight junctions are membrane microdomainsQ40886204
Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structuresQ41231087
Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctionsQ43210831
Tyrosine phosphorylation of occludin attenuates its interactions with ZO-1, ZO-2, and ZO-3.Q44327087
Knockdown of occludin expression leads to diverse phenotypic alterations in epithelial cells.Q45249905
ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation.Q45345068
Differential phosphorylation of occludin and tricellulin by CK2 and CK1.Q45963244
Occludin phosphorylation in regulation of epithelial tight junctions.Q45963248
The oligomerization of the coiled coil-domain of occludin is redox sensitive.Q45963254
Epithelial transport and barrier function in occludin-deficient miceQ46447620
The MARVEL transmembrane motif of occludin mediates oligomerization and targeting to the basolateral surface in epitheliaQ47919576
Oxidized phospholipids mediate occludin expression and phosphorylation in vascular endothelial cells.Q51352759
Post-translational control of occludin membrane assembly in mouse trophectoderm: a mechanism to regulate timing of tight junction biogenesis and blastocyst formation.Q52171417
The tight junction protein occludin and the adherens junction protein alpha-catenin share a common interaction mechanism with ZO-1.Q52941644
A phosphorylation hotspot within the occludin C-terminal domain.Q54506357
Occludin dephosphorylation in early development of Xenopus laevisQ58098095
P4510describes a project that usesImageJQ1659584
P433issue1
P921main subjectphosphorylationQ242736
P304page(s)40
P577publication date2013-06-10
P1433published inCell Communication and SignalingQ1254390
P1476titleCK2-dependent phosphorylation of occludin regulates the interaction with ZO-proteins and tight junction integrity
P478volume11

Reverse relations

cites work (P2860)
Q38629828A role for tight junction-associated MARVEL proteins in larval sea lamprey (Petromyzon marinus) osmoregulation
Q48017174Blood-spinal cord barrier breakdown and pericyte deficiency in peripheral neuropathy
Q39308269Cell Biology of Tight Junction Barrier Regulation and Mucosal Disease
Q51090200Decreased interaction between ZO-1 and occludin is involved in alteration of tight junctions in transplanted epiphora submandibular glands.
Q37458618Effect of wild-type Shigella species and attenuated Shigella vaccine candidates on small intestinal barrier function, antigen trafficking, and cytokine release
Q41835528Generation and quantitative proteomics analysis of CK2α/α'(-/-) cells.
Q33685728Intestinal Epithelial Cell-Specific Deletion of PLD2 Alleviates DSS-Induced Colitis by Regulating Occludin
Q37709043MKP-1 attenuates LPS-induced blood-testis barrier dysfunction and inflammatory response through p38 and IκBα pathways
Q40563819Occludin Content Modulates Hydrogen Peroxide-Induced Increase in Renal Epithelial Paracellular Permeability.
Q42418341Occludin S471 Phosphorylation Contributes to Epithelial Monolayer Maturation.
Q52366670Phosphorylation hotspot in the C-terminal domain of occludin regulates the dynamics of epithelial junctional complexes.
Q47588393Phosphorylation of tight junction transmembrane proteins: Many sites, much to do.
Q38492153Protein kinase CK2 in breast cancer: the CK2β regulatory subunit takes center stage in epithelial plasticity
Q39412884SUMOylation regulates the intracellular fate of ZO-2.
Q38696638Signaling pathways induced by serine proteases to increase intestinal epithelial barrier function.
Q96304481The Effect of Exposure to Bisphenol A on Spermatozoon and the Expression of Tight Junction Protein Occludin in Male Mice
Q39302506The Roles of Glutamine in the Intestine and Its Implication in Intestinal Diseases
Q38223244The role of epithelial tight junctions involved in pathogen infections
Q38706360Tricellulin is a target of the ubiquitin ligase Itch
Q64239829enters gut epithelial cells and impairs intestinal barrier function through cleavage of occludin by serine protease HtrA

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