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Updated: Jan 23, 2026

A Strategy to Validate the Role of Callose-mediated Plasmodesmal Gating in the Tropic Response
Published on: April 17, 2016
Sphingolipid biosynthesis modulates plasmodesmal ultrastructure and phloem unloading
Dawei Yan1, Shri Ram Yadav2,3, Andrea Paterlini1
1The Sainsbury Laboratory, University of Cambridge, Cambridge, UK.
A novel gene, PHLOEM UNLOADING MODULATOR (PLM), regulates organic substance transport in plants. Its absence enhances symplastic transport by affecting plasmodesmal structure, revealing a role for sphingolipids in phloem unloading.
Area of Science:
- Plant biology
- Molecular biology
- Cell biology
Background:
- Phloem unloading is crucial for distributing organic substances to plant sinks like root meristems.
- While initial unloading from sieve elements is understood, post-sieve element transport remains largely uncharacterized.
- Understanding these later stages is key to optimizing nutrient allocation in plants.
Purpose of the Study:
- To identify novel genes involved in post-sieve element phloem unloading.
- To elucidate the molecular mechanisms regulating plasmodesmal function during unloading.
- To investigate the role of sphingolipid metabolism in controlling intercellular transport.
Main Methods:
- Genetic analysis of a novel mutant exhibiting altered phloem unloading.
- Microscopic examination of plasmodesmal structure and endoplasmic reticulum-plasma membrane tethers.
- Biochemical analysis of sphingolipid biosynthesis pathways.
Main Results:
- A novel gene, PHLOEM UNLOADING MODULATOR (PLM), was identified.
- Absence of PLM enhances plasmodesmata-mediated symplastic transport at the pericycle-endodermis interface.
- PLM deficiency disrupts endoplasmic reticulum-plasma membrane tether formation, leading to plasmodesmata lacking cytoplasmic sleeves.
- PLM encodes an enzyme involved in very-long-chain fatty acid sphingolipid biosynthesis.
Conclusions:
- Post-sieve element unloading is regulated by sphingolipid metabolism.
- Sphingolipid metabolism influences plasmodesmal ultrastructure and function.
- The study reveals a novel mechanism controlling intercellular transport and raises questions about plasmodesmata lacking cytoplasmic sleeves.
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