Parallel auxin transport via PINs and plasmodesmata during the Arabidopsis leaf hyponasty response

Plant Cell Rep. 2023 Dec 20;43(1):4. doi: 10.1007/s00299-023-03119-1.

Abstract

The leaf hyponasty response depends on tip-to-petiole auxin transport. This transport can happen through two parallel pathways: active trans-membrane transport mediated by PIN proteins and passive diffusion through plasmodesmata. A plant's ability to counteract potential shading by neighboring plants depends on transport of the hormone auxin. Neighbor sensing at the leaf tip triggers auxin production. Once this auxin reaches the abaxial petiole epidermis, it causes cell elongation, which leads to leaf hyponasty. Two pathways are known to contribute to this intercellular tip-to-petiole auxin movement: (i) transport facilitated by plasma membrane-localized PIN auxin transporters and (ii) diffusion enabled by plasmodesmata. We tested if these two modes of transport are arranged sequentially or in parallel. Moreover, we investigated if they are functionally linked. Mutants in which one of the two pathways is disrupted indicated that both pathways are necessary for a full hyponasty response. Visualization of PIN3-GFP and PIN7-GFP localization indicated PIN-mediated transport in parallel to plasmodesmata-mediated transport along abaxial midrib epidermis cells. We found plasmodesmata-mediated cell coupling in the pin3pin4pin7 mutant to match wild-type levels, indicating no redundancy between pathways. Similarly, PIN3, PIN4 and PIN7 mRNA levels were unaffected in a mutant with disrupted plasmodesmata pathway. Our results provide mechanistic insight on leaf hyponasty, which might facilitate the manipulation of the shade avoidance response in crops.

Keywords: Auxin channeling; Auxin transporter; Diffusion; Leaf angle; Neighbor detection; Shade avoidance response.

MeSH terms

  • Arabidopsis* / genetics
  • Biological Transport
  • Indoleacetic Acids
  • Membrane Transport Proteins / genetics
  • Plasmodesmata

Substances

  • Membrane Transport Proteins
  • Indoleacetic Acids