The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion

• Published in: International journal of molecular sciences Vol. 21; no. 5; p. 1659
• Main Authors: Dubiel, Malgorzata, De Coninck, Tibo, Osterne, Vinicius Jose Silva, Verbeke, Isabel, Van Damme, Daniël, Smagghe, Guy, Van Damme, Els J M
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 28-02-2020; MDPI
• Subjects: Amino Acid Sequence; Apoplast; arabidopsis; Arabidopsis - metabolism; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - metabolism; aratheuls3; Autophagy; Bioinformatics; Cell Nucleus - metabolism; Cyclin-dependent kinases; Cytoplasm; Cytoplasmic Granules - metabolism; Enzymes; Granular materials; Green Fluorescent Proteins - metabolism; intrinsically disordered regions; Kinases; Lectins; Lectins - chemistry; Lectins - metabolism; Localization; mRNA; Peptides; plant lectin; Plasmolysis; Protein Binding; Protein folding; Proteins; Secretion; Storage units; stress granules; Stress, Physiological; Structure-function relationships; Tobacco; Translation; unconventional protein secretion; ArathEULS3; stress granules; unconventional protein secretion; plant lectin; Arabidopsis; intrinsically disordered regions
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms21051659

Stress granules are cytoplasmic compartments, which serve as mRNA storage units during stress, therefore regulating translation. The
lectin
has been widely described as a stress inducible gene. This study aimed to examine in detail the localization of ArathEULS3 lectin in normal and stressed cells. Colocalization experiments revealed that the nucleo-cytoplasmic lectin ArathEULS3 relocates to stress granules after stress. The ArathEULS3 sequence encodes a protein with a EUL lectin domain and an N-terminal domain with unknown structure and function. Bioinformatics analyses showed that the N-terminal domain sequence contains intrinsically disordered regions and likely does not exhibit a stable protein fold. Plasmolysis experiments indicated that ArathEULS3 also localizes to the apoplast, suggesting that this protein might follow an unconventional route for secretion. As part of our efforts we also investigated the interactome of ArathEULS3 and identified several putative interaction partners important for the protein translation process.