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Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus.

ABSTRACT: Protein N-glycosylation in the endoplasmic reticulum (ER) and in the Golgi apparatus is an essential process in eukaryotic cells. Although the N-glycosylation pathway in the ER has been shown to regulate protein quality control, salt tolerance, and cellulose biosynthesis in plants, no biological roles have been linked functionally to N-glycan modifications that occur in the Golgi apparatus. Herein, we provide evidence that mutants defective in N-glycan maturation, such as complex glycan 1 (cgl1), are more salt-sensitive than wild type. Salt stress caused growth inhibition, aberrant root-tip morphology, and callose accumulation in cgl1, which were also observed in an ER oligosaccharyltransferase mutant, staurosporin and temperature sensitive 3a (stt3a). Unlike stt3a, cgl1 did not cause constitutive activation of the unfolded protein response. Instead, aberrant modification of the plasma membrane glycoprotein KORRIGAN 1/RADIALLY SWOLLEN 2 (KOR1/RSW2) that is necessary for cellulose biosynthesis occurred in cgl1 and stt3a. Genetic analyses identified specific interactions among rsw2, stt3a, and cgl1 mutations, indicating that the function of KOR1/RSW2 protein depends on complex N-glycans. Furthermore, cellulose deficient rsw1-1 and rsw2-1 plants were also salt-sensitive. These results establish that plant protein N-glycosylation functions beyond protein folding in the ER and is necessary for sufficient cell-wall formation under salt stress.

SUBMITTER: Kang JS

PROVIDER: S-EPMC2311335 | biostudies-other | 2008 Apr

REPOSITORIES: biostudies-other

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Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus.

Kang Jae Sook JS Frank Julia J Kang Chang Ho CH Kajiura Hiroyuki H Vikram Meenu M Ueda Akihiro A Kim Sewon S Bahk Jeong Dong JD Triplett Barbara B Fujiyama Kazuhito K Lee Sang Yeol SY von Schaewen Antje A Koiwa Hisashi H

Proceedings of the National Academy of Sciences of the United States of America 20080411 15

Protein N-glycosylation in the endoplasmic reticulum (ER) and in the Golgi apparatus is an essential process in eukaryotic cells. Although the N-glycosylation pathway in the ER has been shown to regulate protein quality control, salt tolerance, and cellulose biosynthesis in plants, no biological roles have been linked functionally to N-glycan modifications that occur in the Golgi apparatus. Herein, we provide evidence that mutants defective in N-glycan maturation, such as complex glycan 1 (cgl1) ...[more]

PMID: 18408158

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Project description:Knowledge of protein subcellular localization assists in the elucidation of protein function and understanding of different biological mechanisms that occur at discrete subcellular niches. Organelle-centric proteomics enables localization of thousands of proteins simultaneously. Although such techniques have successfully allowed organelle protein catalogues to be achieved, they rely on the purification or significant enrichment of the organelle of interest, which is not achievable for many organelles. Incomplete separation of organelles leads to false discoveries, with erroneous assignments. Proteomics methods that measure the distribution patterns of specific organelle markers along density gradients are able to assign proteins of unknown localization based on comigration with known organelle markers, without the need for organelle purification. These methods are greatly enhanced when coupled to sophisticated computational tools. Here we apply and compare multiple approaches to establish a high-confidence data set of Arabidopsis root tissue trans-Golgi network (TGN) proteins. The method employed involves immunoisolations of the TGN, coupled to probability-based organelle proteomics techniques. Specifically, the technique known as LOPIT (localization of organelle protein by isotope tagging), couples density centrifugation with quantitative mass-spectometry-based proteomics using isobaric labeling and targeted methods with semisupervised machine learning methods. We demonstrate that while the immunoisolation method gives rise to a significant data set, the approach is unable to distinguish cargo proteins and persistent contaminants from full-time residents of the TGN. The LOPIT approach, however, returns information about many subcellular niches simultaneously and the steady-state location of proteins. Importantly, therefore, it is able to dissect proteins present in more than one organelle and cargo proteins en route to other cellular destinations from proteins whose steady-state location favors the TGN. Using this approach, we present a robust list of Arabidopsis TGN proteins.

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Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus.

Publications

Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus.

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