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Details on Person Tight junction protein ZO-1 (TJP1, also known as zonula occl...
| Class:Id | Summation:9754661 |
|---|---|
| _displayName | Tight junction protein ZO-1 (TJP1, also known as zonula occl... |
| _timestamp | 2021-12-24 20:55:02 |
| created | [InstanceEdit:9754648] Shamovsky, Veronica, 2021-09-30 |
| literatureReference | [LiteratureReference:9754645] Host PDZ-containing proteins targeted by SARS-CoV-2 [LiteratureReference:9754663] SARS-CoV-2 Envelope (E) protein interacts with PDZ-domain-2 of host tight junction protein ZO1 [LiteratureReference:9754646] Long-Term Modeling of SARS-CoV-2 Infection of In Vitro Cultured Polarized Human Airway Epithelium [LiteratureReference:9754667] Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1 [LiteratureReference:9754618] Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers |
| modified | [InstanceEdit:9756268] Shamovsky, Veronica, 2021-10-12 [InstanceEdit:9760735] Shamovsky, Veronica, 2021-12-24 |
| text | Tight junction protein ZO-1 (TJP1, also known as zonula occludens-1) acts a scaffolding protein that regulates the formation of tight junction complexes. TJP1 scaffolding function is crucial for the establishment and maintenance of epithelial polarity and barrier formation in mammals. TJP1 has three PSD-95/Dlg/ZO-1 (PDZ) domains that promote multiple protein-protein interactions. A functional PDZ domain-binding motif has been identified at the carboxy-terminus end of SARS-CoV-2 E (Caillet-Saguy C et al. 2021; Chai J et al. 2021; Shepley-McTaggart A et al. 2021). NMR spectroscopy identified the pentameric structure of transmembrane domain of SARS‐CoV‐2 E protein in lipid bilayers (Mandala VS et al. 2020). Glutathione S-transferase (GST)-fusion protein technique and homogeneous time resolve fluorescence showed that the SARS-CoV-2 E protein interacts with PDZ domain # 2 of TJP1 (Shepley-McTaggart A et al. 2021). A high‐throughput approach of affinity‐profiling against the full human PDZome identified TJP1 and other human PDZ-containing proteins as interactors of SARS-CoV-2 E (Caillet-Saguy C et al. 2021). Further, SARS-CoV-2 infection was found to distort the TJP1 expression causing barrier dysfunction in vitro-cultured polarized human airway epithelium (Hao S et al. 2020). TJP1 knockdown by siRNA transfection in human lung A549 cells slightly increased SARS‐CoV‐2 replication (Caillet-Saguy C et al. 2021). These findings suggest that SARS-CoV-2 infection targets PDZ-containing TJP1 that is recognized by the viral E protein. This Reactome event describes interaction between human TJP1 and SARS-CoV-2 E at the ER-Golgi intermediate compartment (ERGIC) where E localizes for viral assembly and budding. However, additional studies are needed to verify this interaction at ERGIC in vivo experiments. |
| (summation) | [Reaction:9754644] SARS-CoV-2 E pentamer binds TJP1 [Homo sapiens] |
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