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May 2, 20261 citations

Built different: ER cisternae formed by the Arabidopsis Lunapark proteins differ in ultrastructure and affect ER-Golgi transport.

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CPCharlotte PainTRTatiana Spatola RossiNFNadine Field

Key Points

  • This research aims to investigate the structural differences in ER cisternae formed by Lunapark proteins and their impact on ER-Golgi transport.
  • Utilized high-resolution confocal and variable-angle epifluorescence microscopy, transmission electron microscopy, and tomography.
  • Analyzed high-pressure frozen samples of Arabidopsis thaliana.
  • Investigated the effects of AtLNP1 and AtLNP2 on cisternae organization and Golgi morphology.
  • AtLNP1 forms cisternae with dense tubular matrices, while AtLNP2 yields uniform, sac-like structures.
  • Overexpression of AtLNP proteins significantly alters Golgi morphology, impacting ER-to-Golgi transport and secretion.
  • Demonstrated that the balance between AtLNP1 and AtLNP2 is crucial for the organization and functionality of ER cisternae.

Abstract

The plant endoplasmic reticulum (ER) is a dynamic organelle composed of multiple distinct structural domains, such as cisternae, which are maintained by ER morphogens including the Arabidopsis thaliana Lunapark proteins (LNPs). Cisternae are typically described as sac-like structures connected by tubules. Here we challenge this assumption and propose that cisternae have a more complex structure that modifies ER functionality. This study used state-of-the-art high-resolution confocal and variable-angle epifluorescence microscopy, along with transmission electron microscopy and tomography, on high-pressure frozen Arabidopsis thaliana samples. We found that AtLNP1-stabilised ER forms cisternae composed of dense tubular matrices, whereas AtLNP2 forms cisternae with a uniform, sac-like structure. Furthermore, overexpression of AtLNP proteins alters Golgi morphology, affecting ER-to-Golgi transport and secretion. Our findings reveal that the balance between AtLNP1 and AtLNP2 is critical for ER cisternae organisation and ER functionality in protein production and secretion. This work provides new insights into ER structural plasticity and its functional implications in plant cells.

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Cite This Study

Pain et al. (2026) studied this question.

synapsesocial.com/papers/69f594ca71405d493afffa9dhttps://doi.org/10.1111/nph.71217
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