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Cytosolic PINK1 orchestrates protein translation during proteasomal stress by phosphorylating the translation elongation factor eEF1A1
Author(s) -
Qin Siyue,
Ye Ling,
Zheng Youshi,
Gao Ju
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14030
Subject(s) - pink1 , mitophagy , microbiology and biotechnology , phosphorylation , eukaryotic translation elongation factor 1 alpha 1 , proteasome , translation (biology) , elongation factor , protein biosynthesis , kinase , biology , chemistry , biochemistry , ribosome , apoptosis , messenger rna , autophagy , gene , rna
Mutations in PINK1 (PTEN‐induced putative kinase 1) are associated with autosomal recessive early‐onset Parkinson's disease. Full‐length PINK1 (PINK1‐l) has been extensively studied in mitophagy; however, the functions of the short form of PINK1 (PINK1‐s) remain poorly understood. Here, we report that PINK1‐s is recruited to ribosome fractions after short‐term inhibition of proteasomes. The expression of PINK1‐s greatly inhibits protein synthesis even without proteasomal stress. Mechanistically, PINK1‐s phosphorylates the translation elongation factor eEF1A1 during proteasome inhibition. The expression of the phosphorylation mimic mutation eEF1A1S396E rescues protein synthesis defects and cell viability caused by PINK1 knockout. These findings implicate an important role for PINK1‐s in protecting cells against proteasome stress through inhibiting protein synthesis.