Microtubule-based vesicle trafficking usually relies upon kinesin and dynein motors and few reports describe microtubule polymerisation driving directional vesicle trafficking. Here we show that Arabidopsis END BINDING1b (EB1b), a microtubule plus-end binding protein, directly interacts with SYP121, a SNARE protein that mediates the trafficking of the K + channel KAT1 and its distribution to the plasma membrane (PM) in Arabidopsis guard cells. Knockout of AtEB1b and its homologous proteins results in a modest but significant change in the distribution of KAT1 and SYP121 in guard cells and consequently delays light-induced stomatal opening. Live-cell imaging reveals that a portion of SYP121-associated endomembrane compartments co-localise with AtEB1b at the growing ends of microtubules, trafficking along with the growth of microtubules for targeting to the PM. Our study reveals a mechanism of vesicle trafficking driven by microtubule growth, which is involved in the redistribution of PM proteins to modulate guard cell movement.
Keyphrases
- binding protein
- induced apoptosis
- particulate matter
- transcription factor
- air pollution
- cell cycle arrest
- heavy metals
- polycyclic aromatic hydrocarbons
- single cell
- high resolution
- endoplasmic reticulum stress
- emergency department
- water soluble
- cell wall
- drug delivery
- cell proliferation
- protein protein
- amino acid
- plant growth
- endoscopic submucosal dissection