Identifiers
occludin
HUGO:OCLN HGNC:8104 ENTREZ:100506658 UNIPROT:Q16625 GENECARDS:OCLN REACTOME:60846 KEGG:100506658 ATLASONC:GC_OCLN WIKI:OCLN
Maps_Modules
EMT / EMT_REGULATORS
EMT / CELL_CELL_ADHESIONS
EMT / TIGHT_JUNCTIONS
References
PMID:15761153
Occludin is a structural component of tight junctions that is associated with the cell polarity network.
Occludin regulates TGFBR1 localization for efficient TGFB-dependent dissolution of tight junctions during EMT
Interaction of endogenous OCLN with endogenous TGFBR1 was not modulated by TGFB
but its association with the TGFBR2 increased in a TGFB-dependent manner
PMID:15761148
TGFBR1 localizes with ZO-1 on the cellular apical aspect together with PARD6A and they are situated apically to endogenous E-cadherin
After stimulation by TGFB, TGFBR2 is redistributed to the tight junctions, where it localizes with both TGFBR1 and ZO-1.
PMID:22315516
-Occludin is phosphorylated at S340 by PKC
-Occludin is phosphorylated at T383 and S508 by ROCK
-Occludin is phosphorylated at Y398, Y402 and Y 474 by SRC
-Occludin is phosphorylated at T400, T404 and S408 by CK2
-Occludin is phosphorylated at S403 and S404 by PKC-N
-Occludin is phosphorylated at T424 and T438 by PKC-E
-Occludin is phosphorylated at S490 by VEGF
Occludin*@Cytoplasm
Maps_Modules
EMT / EMT_REGULATORS
EMT / CELL_CELL_ADHESIONS
EMT / TIGHT_JUNCTIONS
References
e_re340( EMT ):
PMID:15761153
Occludin is a structural component of tight junctions that is associated with the cell polarity network.
Occludin regulates TGFBR1 localization for efficient TGFB-dependent dissolution of tight junctions during EMT
Interaction of endogenous OCLN with endogenous TGFBR1 was not modulated by TGFB
but its association with the TGFBR2 increased in a TGFB-dependent manner
PMID:15761148
TGFBR1 localizes with ZO-1 on the cellular apical aspect together with PARD6A and they are situated apically to endogenous E-cadherin
After stimulation by TGFB, TGFBR2 is redistributed to the tight junctions, where it localizes with both TGFBR1 and ZO-1.
e_re474( EMT ):
PMID:22315516
-Occludin is phosphorylated at S340 by PKC
-Occludin is phosphorylated at T383 and S508 by ROCK
-Occludin is phosphorylated at Y398, Y402 and Y474 by SRC
-Occludin is phosphorylated at T400, T404 and S408 by CK2
-Occludin is phosphorylated at S403 and S404 by PKC-N
-Occludin is phosphorylated at T424 and T438 by PKC-E
-Occludin is phosphorylated at S490 by VEGF
PMID:19017651
PMID:12604349
In mouse, phosphorylation of Occludin by SRC (at Y398, Y402) reduces TIGHT_JUNCTIONS assembly
In mouse, phosphorylation of Occludin by SRC (at Y398, Y402) reduces interaction between Occludin and ZO1,2,3
PMID:20152177
In mouse, phosphorylation of Occludin by SRC (at Y474) increases interaction between Occludin and PI3K
In mouse, phosphorylation of Occludin by SRC (at Y474) increases wound healing and migration
PMID:12547828
Inactive Src delays the oxidative stress-induced disruption of tight junction and accelerates calcium- induced assembly of tight junction in Caco-2 cells.
This demonstrates that oxidative stress-induced disruption of tight junction is mediated by the activation of Src.
e_re516( EMT ):
PMID:15383321
MTDH is so-called LYRIC
LYRIC colocalizes with ZO1 and Occludin in polarized epithelial cells.
This protein is most likely not involved in the TJ formation as a structural component.
However, it is required for the maturation of the TJ complex
e_re518( EMT ):
PMID:22671595
Caveolin-1 is an endocytic scaffolding protein
It binds independently to claudin-2 and occludin (co-immunoprecipitation assays).
The finding that caveolin-1 interacts with claudin-2 and occludin, but notwith claudin-4 or ZO-1, suggests a potential mechanism for selective retrieval of tight junction components.
e_re651( EMT ):
PMID:11978007
Cx32 Formation and / or Cx32-Mediated Intercellular Communication Induces Expression and Function of Tight Junctions in Hepatocytic Cell Line
PMID:10581193
Induction of tight junctions in human connexin 32-transfected mouse hepatocytes: connexin 32 interacts with occludin.
PMID:17568974
Connexins induce and maintain tight junctions in epithelial cells.
Occludin*@Extracellular space
Maps_Modules
EMT / EMT_REGULATORS
EMT / CELL_CELL_ADHESIONS
EMT / TIGHT_JUNCTIONS
Occludin*|pho@Cytoplasm
Maps_Modules
EMT / EMT_REGULATORS
EMT / CELL_CELL_ADHESIONS
EMT / TIGHT_JUNCTIONS
References
e_re474( EMT ):
PMID:22315516
-Occludin is phosphorylated at S340 by PKC
-Occludin is phosphorylated at T383 and S508 by ROCK
-Occludin is phosphorylated at Y398, Y402 and Y474 by SRC
-Occludin is phosphorylated at T400, T404 and S408 by CK2
-Occludin is phosphorylated at S403 and S404 by PKC-N
-Occludin is phosphorylated at T424 and T438 by PKC-E
-Occludin is phosphorylated at S490 by VEGF
PMID:19017651
PMID:12604349
In mouse, phosphorylation of Occludin by SRC (at Y398, Y402) reduces TIGHT_JUNCTIONS assembly
In mouse, phosphorylation of Occludin by SRC (at Y398, Y402) reduces interaction between Occludin and ZO1,2,3
PMID:20152177
In mouse, phosphorylation of Occludin by SRC (at Y474) increases interaction between Occludin and PI3K
In mouse, phosphorylation of Occludin by SRC (at Y474) increases wound healing and migration
PMID:12547828
Inactive Src delays the oxidative stress-induced disruption of tight junction and accelerates calcium- induced assembly of tight junction in Caco-2 cells.
This demonstrates that oxidative stress-induced disruption of tight junction is mediated by the activation of Src.
Modifications:
In compartment: Cytoplasm
In compartment: Extracellular space
Participates in complexes:
In compartment: Cytoplasm
- GJB1:Occludin*@Cytoplasm
- LYRIC*:Occludin*@Cytoplasm
- Nectin*:Occludin*@Cytoplasm
- Cingulin*:Occludin*@Cytoplasm
- Claudin1*:Occludin*@Cytoplasm
- Claudin2*:Occludin*@Cytoplasm
- Caveolin1*:Occludin*@Cytoplasm
- Actin cytoskeletal*:Occludin*@Cytoplasm
- Occludin*:PARD6A:TGFBR1|hm2@Cytoplasm
- Occludin*:PARD6A:TGFB1|hm2:TGFBR1|hm2:TGFBR2|hm2@Cytoplasm
- Occludin*:PARD6A|S345_pho:TGFB1|hm2:TGFBR1|Ser_pho|hm2:TGFBR2|Ser_pho|hm2@Cytoplasm
Participates in reactions:
As Reactant or Product:
- PARD6A@Cytoplasm
+ TGFBR1|hm2@Cytoplasm
+ Occludin*@Cytoplasm
→
Occludin*:PARD6A:TGFBR1|hm2@Cytoplasm
- Occludin*:PARD6A:TGFB1|hm2:TGFBR1|hm2:TGFBR2|hm2@Cytoplasm
+ ATP@Cytoplasm
→
Occludin*:PARD6A|S345_pho:TGFB1|hm2:TGFBR1|Ser_pho|hm2:TGFBR2|Ser_pho|hm2@Cytoplasm
+ ADP@Cytoplasm
- Occludin*:PARD6A:TGFBR1|hm2@Cytoplasm
+ TGFB1|hm2:TGFBR1|hm2:TGFBR2|hm2@Cytoplasm
→
Occludin*:PARD6A:TGFB1|hm2:TGFBR1|hm2:TGFBR2|hm2@Cytoplasm
- Occludin*:PARD6A|S345_pho:TGFB1|hm2:TGFBR1|Ser_pho|hm2:TGFBR2|Ser_pho|hm2@Cytoplasm
+ SMURF1@Cytoplasm
→
PARD6A|S345_pho:SMURF1@Cytoplasm
- rOccludin*@Nucleus
→
Occludin*@Cytoplasm
- Occludin*@Cytoplasm
+ ATP@Cytoplasm
→
Occludin*|pho@Cytoplasm
+ ADP@Cytoplasm
- Occludin*@Extracellular space
+ Occludin*@Cytoplasm
→
Occludin*|hm2@Extracellular space
- Occludin*@Cytoplasm
+ Claudin1*@Cytoplasm
→
Claudin1*:Occludin*@Cytoplasm
- Occludin*@Cytoplasm
+ Claudin2*@Cytoplasm
→
Claudin2*:Occludin*@Cytoplasm
- Occludin*@Cytoplasm
+ Cingulin*@Cytoplasm
→
Cingulin*:Occludin*@Cytoplasm
- Occludin*@Cytoplasm
+ Nectin*@Cytoplasm
→
Nectin*:Occludin*@Cytoplasm
- LYRIC*@Cytoplasm
+ Occludin*@Cytoplasm
→
LYRIC*:Occludin*@Cytoplasm
- Occludin*@Cytoplasm
+ Actin cytoskeletal*@Cytoplasm
→
Actin cytoskeletal*:Occludin*@Cytoplasm
- Occludin*@Cytoplasm
+ Caveolin1*@Cytoplasm
→
Caveolin1*:Occludin*@Cytoplasm
- Occludin_Claudin1_2_4_5_7_8_16*@Cytoplasm
→
Occludin*@Cytoplasm
- Occludin*|hm2@Extracellular space
→
Tight junctions@Extracellular space
- Claudin1*:Occludin*@Cytoplasm
→
Tight junctions@Extracellular space
- Claudin2*:Occludin*@Cytoplasm
→
Tight junctions@Extracellular space
- Actin cytoskeletal*:Occludin*@Cytoplasm
→
Tight junctions@Extracellular space
- Occludin*@Cytoplasm
+ GJB1@Cytoplasm
→
GJB1:Occludin*@Cytoplasm
- GJB1:Occludin*@Cytoplasm
→
Tight junctions@Extracellular space
As Catalyser: