ArticleMolecular biology of the cell2013
The intracellular fate of zonula occludens 2 is regulated by the phosphorylation of SR repeats and the phosphorylation/O-GlcNAcylation of S257.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- ZO-2 is a scaffold at the centriole and mitotic spindle poles that enhances microtubule stability and supports the proper development of mitotic spindles and cilia.Cell and tissue research · 2025Article
- The Role of ZO-2 in Modulating JAM-A and γ-Actin Junctional Recruitment, Apical Membrane and Tight Junction Tension, and Cell Response to Substrate Stiffness and Topography.International journal of molecular sciences · 2024Article
- Serine-arginine protein kinases and their targets in viral infection and their inhibition.Cellular and molecular life sciences : CMLS · 2023Review
- Working a second job: Cell adhesion proteins that moonlight in the nucleus.Frontiers in cell and developmental biology · 2023Review
- SR Protein Kinase 1 Inhibition by TAF15.Cells · 2022Article
- Article
- ZO-2 favors Hippo signaling, and its re-expression in the steatotic liver by AMPK restores junctional sealing.Tissue barriers · 2022Article
- Good Cop, Bad Cop: The Different Roles of SRPKs.Frontiers in genetics · 2022Review
- YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.International journal of molecular sciences · 2021Article
- Article
- Tight junction protein ZO-2 modulates the nuclear accumulation of transcription factor TEAD.Molecular biology of the cell · 2021Article
- Article
- ZO-2 Is a Master Regulator of Gene Expression, Cell Proliferation, Cytoarchitecture, and Cell Size.International journal of molecular sciences · 2019Review
- Activation of the CaMolecular biology of the cell · 2019Article
- SUMOylation regulates the intracellular fate of ZO-2.Cellular and molecular life sciences : CMLS · 2017Article
- ZO-2 silencing induces renal hypertrophy through a cell cycle mechanism and the activation of YAP and the mTOR pathway.Molecular biology of the cell · 2016Article
- Progressive Hearing Loss in Mice Carrying a Mutation in Usp53.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- RhoGTPases, actomyosin signaling and regulation of the epithelial Apical Junctional Complex.Seminars in cell & developmental biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zona occludens 2 (ZO-2) has a dual localization. In confluent epithelia, ZO-2 is present at tight junctions (TJs), whereas in sparse proliferating cells it is also found at the nucleus. Previously we demonstrated that in sparse cultures, newly synthesized ZO-2 travels to the nucleus before reaching the plasma membrane. Now we find that in confluent cultures newly synthesized ZO-2 goes directly to the plasma membrane. Epidermal growth factor induces through AKT activation the phosphorylation of the kinase for SR repeats, serine arginine protein kinase 1, which in turn phosphorylates ZO-2, which contains 16 SR repeats. This phosphorylation induces ZO-2 entry into the nucleus and accumulation in speckles. ZO-2 departure from the nucleus requires intact S257, and stabilizing the β-O-linked N-acetylglucosylation (O-GlcNAc) of S257 with O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate, an inhibitor of O-GlcNAcase, triggers nuclear exportation and proteosomal degradation of ZO-2. At the plasma membrane ZO-2 is not O-GlcNAc, and instead, as TJs mature, it becomes phosphorylated at S257 by protein kinase Cζ. This late phosphorylation of S257 is required for the correct cytoarchitecture to develop, as cells transfected with ZO-2 mutant S257A or S257E form aberrant cysts with multiple lumens. These results reveal novel posttranslational modifications of ZO-2 that regulate the intracellular fate of this protein.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.