Hiring in life sciences? Share your open positions with our professional community. Read more Close

Advertisement

Poly(A)-binding proteins act as a thermosensory switch to control flowering via cytoplasmic retention of RNA-binding protein 45C.

Created on 01 Aug 2026

Authors

An Yan, Ximing Gong, Songyao Zhang, Jiahui Chen, Hao Yu

Published in

Science advances. Volume 12. Issue 31. Pages eaeg8264. Jul 31, 2026. Epub Jul 31, 2026.

Abstract

Poly(A)-binding proteins (PABPs) are canonically recognized for their roles in mRNA-dependent processes through binding to the poly(A) tail of mRNA. However, whether PABPs possess functions distinct from their action on mRNA, particularly in controlling major developmental transitions, has remained unexplored. Here, we uncover a hitherto unknown role for two PABPs, PAB2 and PAB8, in flowering time control in Arabidopsis thaliana. We demonstrate that PAB2 and PAB8 interact with RNA-binding protein 45C (RBP45C) and determine its cytoplasmic retention. This prevents nuclear entry of RBP45C and its function in promoting the transcription and splicing of the key floral repressor FLOWERING LOCUS C (FLC). Furthermore, low ambient temperature attenuates the interaction between PAB2 and RBP45C, resulting in late flowering attributable to compromised cytoplasmic retention of RBP45C and elevated FLC expression. Our findings identify a non-canonical role of PABPs as a cytoplasmic anchor for RBP45C, which serves as a thermosensory switch of FLC expression to fine-tune flowering in response to cool ambient temperature.

PMID:
42536759
Bibliographic data and abstract were imported from PubMed on 01 Aug 2026.

Read full publication at:
Please sign in to see all details.

Advertisement

Stats

  • Community rating n/a 0 votes
  • Reviewers' rating n/a 0 votes
  • Your rating

1-terrible, 9-excellent. How would you rate this publication? Sign in in to submit your rating.

  • Recommendations n/a n/a positive of 0 vote(s)
  • Views 7
  • Comments 0

Recommended by

  • No recommendations yet.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.

Advertisement