Abstract
BackgroundTo cope with harsh environments, crustaceans such as Artemia produce diapause gastrula embryos (cysts) with suppressed metabolism. Metabolism and development resume during post-diapause development, but the mechanism behind these cellular events remains largely unknown.Principal FindingOur study investigated the role of prohibitin 1 (PHB1) in metabolic reinitiation during post-diapause development. We found that PHB1 was developmentally regulated via changes in phosphorylation status and localization. Results from RNA interference experiments demonstrated PHB1 to be critical for mitochondrial maturation and yolk degradation during development. In addition, PHB1 was present in yolk platelets, and it underwent ubiquitin-mediated degradation during the proteolysis of yolk protein.Conclusions/SignificancePHB1 has an indispensable role in coordinating mitochondrial maturation and yolk platelet degradation during development in Artemia. This novel function of PHB1 provides new clues to comprehend the roles of PHB1 in metabolism and development.
Highlights
Prohibitin 1 (PHB1), a prohibitin family protein, forms a large complex with PHB2 at the inner mitochondrial membrane
To investigate the role of ArPHB1 in the development of Artemia, a 988-bp cDNA encoding ArPHB1 was cloned by polymerase chain reaction (PCR) from post-diapause embryos of A. parthenogenetica from Gahai Lake using DF1, DF2, DR1, and DR2 primers for degenerate PCR and 3F1, 3F2, 5R1, and 5R2 primers for the rapid amplification of cDNA ends (Table S1)
The deduced amino acid sequence showed that ArPHB1 had a conserved prohibitin domain, a coiled-coil domain, an Nterminal hydrophobic sequence, and a nuclear export sequence (NES) (Fig. 1A)
Summary
Prohibitin 1 (PHB1), a prohibitin family protein, forms a large complex with PHB2 at the inner mitochondrial membrane. PHB1 regulates transcription in the nucleus by interacting with E2F, retinoblastoma protein (Rb), and chromatin-remodeling complexes (Brg-1/Brm). Phosphorylation of PHB1 results in its association with the plasma membrane, activation of the Ras–Raf signaling pathway, which regulates epithelial cell adhesion and migration [8], and metastasis [9]. In light of these findings, PHB1 is a promising target for clinical applications because natural anticancer compounds such as rocaglamide can inhibit the Ras2Raf signaling pathway by binding to PHB1 [10]. PHB1 was present in yolk platelets, and it underwent ubiquitin-mediated degradation during the proteolysis of yolk protein
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