Phosphorylation of G3BP1-S149 does not influence stress granule assembly

Marc D Panas; Nancy Kedersha; Tim Schulte; Rui M Branca; Pavel Ivanov; Paul Anderson

doi:10.1083/jcb.201801214

Phosphorylation of G3BP1-S149 does not influence stress granule assembly

J Cell Biol. 2019 Jul 1;218(7):2425-2432. doi: 10.1083/jcb.201801214. Epub 2019 Jun 6.

Authors

Marc D Panas^{1

2}, Nancy Kedersha¹, Tim Schulte³, Rui M Branca⁴, Pavel Ivanov¹, Paul Anderson⁵

Affiliations

¹ Division of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA.
² Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden.
³ Science for Life Laboratory, Department of Medicine Solna, Karolinska Institutet, Stockholm, Sweden.
⁴ Clinical Proteomics Mass Spectrometry, Department of Oncology-Pathology, Science for Life Laboratory, Karolinska Institutet, Stockholm, Sweden.
⁵ Division of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA panderson@rics.bwh.harvard.edu.

Abstract

Tourrière et al. (2013. J. Cell Biol. https://doi.org/10.1083/jcb.200212128) reported that G3BP1-S149 dephosphorylation promotes stress granule formation. We show that constructs used to establish this conclusion contain additional mutations causing these phenotypes, and that S149 phosphorylation status does not change upon stress.

Publication types

Letter
Comment

MeSH terms

Carrier Proteins
DNA Helicases*
Endoribonucleases
Phosphorylation
Poly-ADP-Ribose Binding Proteins
RNA Helicases*
RNA Recognition Motif Proteins
ras GTPase-Activating Proteins

Substances

Carrier Proteins
Poly-ADP-Ribose Binding Proteins
RNA Recognition Motif Proteins
ras GTPase-Activating Proteins
Endoribonucleases
DNA Helicases
RNA Helicases

Abstract

Publication types

MeSH terms

Substances

Grants and funding