# Contact and communication: ZO‐2 and the Hippo pathway

**Authors:** Miranda Thomas

PMC · DOI: 10.1111/febs.17417 · The Febs Journal · 2025-02-05

## TL;DR

ZO-2, a protein involved in cell junctions and signaling, acts as a scaffold in the Hippo pathway, helping regulate cellular processes.

## Contribution

The study reveals how ZO-2's multiple protein binding sites enable it to function as a scaffold in signaling pathways.

## Key findings

- ZO-2 has multiple protein binding sites that allow it to act as a scaffold.
- This scaffolding function facilitates ZO-2's role in signaling pathways like the Hippo pathway.

## Abstract

The PDZ domain‐containing protein ZO‐2 is defined as a tight junction (TJ) protein, but is also known to have a role in the maintenance of cellular apicobasal polarity and to function as a signalling molecule in several pathways, including the Hippo pathway. In this issue, Liu OX et al. [(2024) FEBS J, https://doi.org/10.1111/febs.17304] report how the multiple protein binding sites of ZO2 protein allow it to act as a scaffold to facilitate its signalling functions.

The PDZ domain‐containing protein ZO‐2 is defined as a tight junction protein, but is also known to play a role in the maintenance of cellular apicobasal polarity, and to function as a signalling molecule in several pathways, including the Hippo pathway. Liu et al. report how the multiple protein binding sites of ZO‐2 protein enable it to act as a scaffold, thereby facilitating its signalling functions.

Comment on: https://doi.org/10.1111/febs.17304.

## Linked entities

- **Proteins:** TJP2 (tight junction protein 2)

## Full-text entities

- **Genes:** TJP2 (tight junction protein 2) [NCBI Gene 9414] {aka C9DUPq21.11, DFNA51, DUP9q21.11, FHCA1, PFIC4, X104}

## Full text

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## Figures

1 figure with captions in the complete paper: https://tomesphere.com/paper/PMC11970711/full.md

## References

11 references — full list in the complete paper: https://tomesphere.com/paper/PMC11970711/full.md

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Source: https://tomesphere.com/paper/PMC11970711