A-kinase anchoring protein 8L interacts with mTORC1 and promotes cell growth

Chase H. Melick, Delong Meng, Jenna L. Jewell

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The mammalian target of rapamycin complex 1 (mTORC1) senses nutrients to mediate anabolic processes within the cell. Exactly how mTORC1 promotes cell growth remains unclear. Here, we identified a novel mTORC1-interacting protein called A-kinase anchoring protein 8L (AKAP8L). Using biochemical assays, we found that the N-terminal region of AKAP8L binds to mTORC1 in the cytoplasm. Importantly, loss of AKAP8L decreased mTORC1-mediated processes such as translation, cell growth and cell proliferation. AKAPs anchor protein kinase A (PKA) through PKA regulatory subunits, and we show that AKAP8L can anchor PKA through regulatory subunit Ia. Reintroducing full-length AKAP8L into cells restored mTORC1-regulated activities, whereas reintroduction of AKAP8L missing the N-terminal region that confers the interaction with mTORC1 did not. Our results suggest a multifaceted role for AKAPs in the cell. We conclude that mTORC1 appears to regulate protein translation, perhaps in part through AKAP8L.

Original languageEnglish (US)
JournalJournal of Biological Chemistry
Volume295
Issue number23
DOIs
StatePublished - Apr 2020

Keywords

  • A-kinase anchoring protein (AKAP)
  • AKAP8L
  • Anabolic pathway
  • CAMP signaling
  • Cell proliferation
  • Cell size
  • MRNA translation
  • MTORC1
  • Nutrient sensing
  • Scaffolding protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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