NLA proteins: Master regulators that integrate nutrient homeostasis, stress adaptation, and plant development

Clicks: 27
ID: 329127
2026
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 #62 of 401 articles by views in Journal of experimental botany

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 401 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
Abstract
Abstract As sessile organisms, plants rely on intricate molecular regulatory networks to navigate complex, fluctuating environments and diverse stress conditions. Nitrogen Limitation Adaptation (NLA), a RING-type ubiquitin ligase harboring an SPX domain, has emerged as a central hub integrating plant responses to nutrient availability, pathogen attack, and cold stress. This review provides a systematic overview of the structural features of NLA, with a particular focus on the regulatory role of inositol pyrophosphates (PP-InsPs) in plant phosphorus signaling. We highlight the core functions of NLA in maintaining nitrogen–phosphorus homeostasis and mediating the crosstalk between nutrient status and immune defense. A key mechanism we discuss is the role of maize ZmNLA in "cold–phosphorus" trade-off, whereby ZmNLA activates jasmonate signaling to enhance cold tolerance by mediating the ubiquitination and degradation of the signaling repressor ZmJAZ11, while simultaneously restricting phosphate uptake via targeting the phosphate transporter ZmPT4. Notably, the ZmNLAΔ12 variant, which has an impaired PP-InsPs binding site, functionally uncouples this trade-off through structure-guided protein design. Finally, we propose future research directions and discuss the potential for breeding new crop varieties with enhanced stress adaptation and improved nutrient use efficiency.
Reference Key
openalex_W7213562963 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors
Journal Journal of experimental botany
Year 2026
DOI
10.1093/jxb/erag476
URL
Keywords Keywords not found

Citations

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

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