Open AccessStress granules as a feedback mechanism of MAPK signaling by sequestering PKC/Pck2
Author(s) -
Yuki Kanda,
Ryuji Satoh,
Teruaki Takasaki,
Naofumi Tomimoto,
Kiko Tsuchiya,
Chun An Tsai,
Taemi Tanaka,
Shu Kyomoto,
Kozo Hamada,
Toshinobu Fujiwara,
Reiko Sugiura
Publication year - 2020
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.250191
Subject(s) - mapk/erk pathway , biology , microbiology and biotechnology , signal transduction , protein kinase c , kinase , cell growth , mitogen activated protein kinase , chromosomal translocation , protein kinase a , cell , cytoplasm , biochemistry , gene
The PKC signaling is a highly conserved signaling module, which plays a central role in a myriad of physiological processes, ranging from cell proliferation to cell death via various signaling pathways, including MAPK. Stress granules (SGs) are non-membranous cytoplasmic foci that aggregate in cells exposed to environmental stresses. Here we explored the role of SGs in PKC/MAPK signaling activation in fission yeast. High heat-stress (HHS) induced Pmk1 MAPK activation and Pck2/PKC translocation from the cell tips into poly(A)-binding protein (Pabp)-positive SGs. Pck2 dispersal from the cell tips required Pck2 kinase activity and the constitutively active Pck2 promotes its translocation to SGs. Importantly, Pmk1 deletion impaired Pck2 recruitment into SGs, indicating that MAPK activation stimulates Pck2 SG translocation. Consistently, HHS-induced SGs delayed Pck2 relocalization at the cell tips, thereby blocking subsequent Pmk1 reactivation after recovery from HHS. HHS partitioned Pck2 into the Pabp-positive SG-containing fraction, which resulted in the reduced Pck2 abundance and kinase activity in the soluble fraction. Collectively, MAPK-dependent Pck2 SG recruitment serves as a feedback mechanism to intercept PKC/MAPK activation induced by HHS, which might underlie PKC-related diseases.