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

Read full text
Authors: Charlotte Pain, Tatiana Spatola Rossi, Nadine Field, Carmen Mata, Alessia Candeo, Muhammad W Ali, Flavia Moreira-Leite, Stanley W. Botchway, Federica Brandizzí, Verena Kriechbaumer
Cited by: 1
References: 71

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.

Fields of Study & Subjects

Cellular transport and secretion Endoplasmic Reticulum Stress and Disease Autophagy in Disease and Therapy

Publication details

Journal / source
New Phytologist
Publisher
Wiley
Volume
250
Issue
6
Pages
3828–3845
Publication date
29 April 2026
Language
EN