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The ArathEULS3 lectin ends up in stress granules and can follow an unconventional route for secretion

Malgorzata Dubiel (UGent) , Tibo De Coninck (UGent) , Vinicius Da Silva Osterne (UGent) , Isabel Verbeke (UGent) , Daniël Van Damme (UGent) , Guy Smagghe (UGent) and Els Van Damme (UGent)
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Abstract
Stress granules are cytoplasmic compartments, which serve as mRNA storage units during stress, therefore regulating translation. The Arabidopsis thaliana lectin ArathEULS3 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.
Keywords
Physical and Theoretical Chemistry, Inorganic Chemistry, Organic Chemistry, Spectroscopy, Molecular Biology, Catalysis, General Medicine, Computer Science Applications, Arabidopsis, ArathEULS3, intrinsically disordered regions, plant lectin, stress granules, unconventional protein secretion, INTRINSICALLY DISORDERED REGIONS, EXTRACELLULAR VESICLES, PROCESSING BODIES, PLANT-LECTINS, ARABIDOPSIS, PROTEIN, COMPONENTS, PREDICTION, DISTINCT, GROWTH

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MLA
Dubiel, Malgorzata, et al. “The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 21, no. 5, 2020.
APA
Dubiel, M., De Coninck, T., Da Silva Osterne, V., Verbeke, I., Van Damme, D., Smagghe, G., & Van Damme, E. (2020). The ArathEULS3 lectin ends up in stress granules and can follow an unconventional route for secretion. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 21(5).
Chicago author-date
Dubiel, Malgorzata, Tibo De Coninck, Vinicius Da Silva Osterne, Isabel Verbeke, Daniël Van Damme, Guy Smagghe, and Els Van Damme. 2020. “The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 21 (5).
Chicago author-date (all authors)
Dubiel, Malgorzata, Tibo De Coninck, Vinicius Da Silva Osterne, Isabel Verbeke, Daniël Van Damme, Guy Smagghe, and Els Van Damme. 2020. “The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 21 (5).
Vancouver
1.
Dubiel M, De Coninck T, Da Silva Osterne V, Verbeke I, Van Damme D, Smagghe G, et al. The ArathEULS3 lectin ends up in stress granules and can follow an unconventional route for secretion. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 2020;21(5).
IEEE
[1]
M. Dubiel et al., “The ArathEULS3 lectin ends up in stress granules and can follow an unconventional route for secretion,” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 21, no. 5, 2020.
@article{8652914,
  abstract     = {Stress granules are cytoplasmic compartments, which serve as mRNA storage units during stress, therefore regulating translation. The Arabidopsis thaliana lectin ArathEULS3 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.},
  articleno    = {1659},
  author       = {Dubiel, Malgorzata and De Coninck, Tibo and Da Silva Osterne, Vinicius and Verbeke, Isabel and Van Damme, Daniël and Smagghe, Guy and Van Damme, Els},
  issn         = {1422-0067},
  journal      = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
  keywords     = {Physical and Theoretical Chemistry,Inorganic Chemistry,Organic Chemistry,Spectroscopy,Molecular Biology,Catalysis,General Medicine,Computer Science Applications,Arabidopsis,ArathEULS3,intrinsically disordered regions,plant lectin,stress granules,unconventional protein secretion,INTRINSICALLY DISORDERED REGIONS,EXTRACELLULAR VESICLES,PROCESSING BODIES,PLANT-LECTINS,ARABIDOPSIS,PROTEIN,COMPONENTS,PREDICTION,DISTINCT,GROWTH},
  language     = {eng},
  number       = {5},
  title        = {The ArathEULS3 lectin ends up in stress granules and can follow an unconventional route for secretion},
  url          = {http://dx.doi.org/10.3390/ijms21051659},
  volume       = {21},
  year         = {2020},
}

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