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Updated: Jan 22, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Molecular identification and diapause-related functional characterization of a novel dual-specificity kinase gene,
Kun Hao1, Hidayat Ullah1,2, Aftab Raza Jarwar1
1State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Abstract:
Diapause is an important overwintering strategy enabling Locusta migratoria to survive under stressed conditions. We identified a novel dual-specificity kinase gene that is differentially expressed between long and short day-treated L. migratoria. To determine its function on photoperiodic diapause induction, we cloned the specific gene. Interestingly, phylogenetic analysis shows that this dual-specificity kinase is of the mycetozoa protein kinase-like (MPKL) type and may have been transferred horizontally from Mycetozoa to L. migratoria. RNA interference results confirm that MPKL promotes photoperiodic diapause induction of L. migratoria. Furthermore, MPKL significantly inhibits Akt and FOXO (i.e. forkhead box protein O) phosphorylation levels in ovaries, and also enhances reactive oxygen species, superoxide dismutase and catalase activities, whereas peroxidase activity is decreased under both photoperiodic regimes. The findings of the present study offer insight into the molecular mechanism responsible for dual-specificity kinase-induced diapause in insects.
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