Decoding BIG: how one protein influences multiple pathways

Clicks: 19
ID: 326591
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
Steady

Ranked #215 of 406 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 406 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
Abstract A major strength of forward genetic screens is their unbiased nature: the plant reveals which genes underlie a physiological process. Yet this strength often presents a new challenge: determining the biochemical basis of the mutant phenotype. BIG/DARK OVEREXPRESSION OF CAB1/TRANSPORT INHIBITOR RESPONSE3 encodes an exceptionally large (∼0.5 MDa) protein identified in diverse genetic screens. big mutants have smaller stature, reduced elongation growth and apical dominance, and defects in lateral root formation, phenotypes consistent with disrupted auxin gradients. However, they also display altered stomatal behaviour, circadian regulation, pathogen responses, and changes in other hormone pathways. This broad pleiotropy points to wide-ranging roles in signalling and development, yet the biochemical function of BIG remained unresolved for more than three decades. Recently, we showed that BIG participates in the Arg/N-degron pathways, a specialised form of proteostasis in which the half-lives of proteins are influenced by their N-terminal (Nt) residues. However, this does not explain the pleiotropic phenotypes of big mutants. New structural and functional clues from the mammalian homologue ubiquitin amino-end recognising protein 4 (UBR4) point to wider proteostatic roles for BIG, providing a potential explanation for the impacts of BIG on plant physiology and a rich source of hypotheses for future studies.
Reference Key
openalex_W7204552647 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Frederica L. Theodoulou, Daniel B. Grabarczyk, Tim Clausen, Andreas Bachmair
Are you one of these authors? Claim your profile
Journal Journal of experimental botany
Year 2026
DOI
10.1093/jxb/erag427
URL
https://doi.org/10.1093/jxb/erag427
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.