TurboID proximity labeling combined with structure prediction identifies C3H61/AtTZF5 as a tail-binding protein of Arabidopsis class VIII myosin ATM1

Clicks: 9
ID: 338788
2026
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Emerging

Ranked #123 of 123 articles by views in plant and cell physiology

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 123 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
Higher plants possess two classes of myosin molecular motors, class XI and class VIII, both unique to the plant lineage. The diverse cellular functions of class XI myosins, including organelle transport and nuclear positioning, have been elucidated largely through systematic identification of cargo adaptor proteins that bind to their globular tail domains (GTDs). In contrast, no proteome-wide screen for class VIII myosin tail-binding proteins has been reported; the few known interacting proteins were each discovered through studies focused on the binding partner rather than on the myosin itself, leaving the full repertoire of class VIII myosin-associated proteins largely unknown. Here, we employed TurboID-based proximity labeling to systematically identify proteins associated with the GTD of the class VIII myosin ATM1 in Arabidopsis thaliana, as this approach covalently biotinylates neighboring proteins in vivo, enabling their identification even after proteolytic degradation during cell lysis. We identified 233 non-redundant candidate ATM1-proximal proteins. Candidates were prioritized by AlphaFold3-based protein complex structure prediction and evaluated experimentally. By integrating AlphaFold3 prediction, co-immunoprecipitation, subcellular co-localization in living cells under stress, and structure-guided interface mutagenesis, we identified C3H61/AtTZF5 as an ATM1 tail-binding protein. C3H61/AtTZF5, a tandem CCCH zinc finger protein whose family members have been implicated in mRNA turnover, co-localized with the ATM1 tail in eIF4A2-positive granules under heat stress, and targeted substitutions at the AlphaFold3-predicted interface completely abolished the interaction. These findings strongly support a direct association between ATM1 and C3H61/AtTZF5, suggesting a possible link between this class VIII myosin and post-transcriptional gene regulation during stress responses.
Reference Key
openalex_W7155525922 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors さくら 永田, Shun Sakuraba, Emi Mishiro-Sato, Takashi L. Shimada, Yuzuki Oe, Kohei Tachibana, Jun Obara, 就也 内田, Motoki Tominaga, Kohji Ito, Takeshi Haraguchi
Are you one of these authors? Claim your profile
Journal plant and cell physiology
Year 2026
DOI
10.1093/pcp/pcag155
URL
https://doi.org/10.1093/pcp/pcag155
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.