AMPK Promotes Larval Metamorphosis of Mytilus coruscus

Abstract

Metamorphosis is a critical process in the transition from planktonic life to benthic life for marine invertebrates, which is accompanied by a large amount of energy consumption. Previous studies have proved that AMP-activated protein kinase (AMPK), as a vital energy regulator, plays a prominent role in mediating the growth and development of terrestrial animals. However, its function in the growth and development of marine invertebrates, especially in metamorphosis, remains elusive. This study explored the function of AMPK in the larval metamorphosis of Mytilus coruscus. The full-length cDNA of AMPK genes in M. coruscus was cloned and characterized, which is composed of three subunits, McAMPKα, McAMPKβ, and McAMPKγ. Pharmacological tests demonstrated that through the application of an AMPK activator, AMP substantially enhanced the larval metamorphosis rate (p < 0.05). By contrast, the larval metamorphosis rate decreased significantly after being treated with the AMPK inhibitor Compound C (p < 0.05). McAMPK gene knock-down resulted in a reduction in McAMPK gene expression (p < 0.05), and the larval metamorphosis of M. coruscus was significantly restrained (p < 0.05). These results indicated that AMPK signaling is vital in the larval metamorphosis of M. coruscus, which advances further understanding in exploring the molecular mechanisms in the metamorphosis of marine invertebrate larvae.

TRPM7-Mediated Ca2+ Regulates Mussel Settlement through the CaMKKβ-AMPK-SGF1 Pathway

“…Recently, more and more studies have indicated that AMPK signaling is vital to the larval settlement and metamorphosis in marine invertebrates including the mussel Mytilus coruscus [ 29 ] and the barnacle Amphibalanus amphitrite [ 30 ], however, the underlying molecular mechanisms are unclear. To further elucidate the biochemical mechanisms by which AMPK regulates the larval settlement of M. sallei , we conducted a yeast two hybrid (Y2H) assay to identify its interacting proteins.…”