RNA helicase SACY-1 is required for longevity caused by various genetic perturbations in Caenorhabditis elegans

Cell Cycle. 2016 Jul 17;15(14):1821-9. doi: 10.1080/15384101.2016.1183845. Epub 2016 May 6.

Abstract

RNA helicases, which unwind RNAs, are essential for RNA metabolism and homeostasis. However, the roles of RNA helicases in specific physiological processes remain poorly understood. We recently reported that an RNA helicase, HEL-1, promotes long lifespan conferred by reduced insulin/insulin-like growth factor-1 (IGF-1) signaling (IIS) in Caenorhabditis elegans. We also showed that HEL-1 induces the expression of longevity genes by physically interacting with Forkhead box O (FOXO) transcription factor. Thus, the HEL-1 RNA helicase appears to regulate lifespan by specifically activating FOXO in IIS. In the current study, we report another longevity-promoting RNA helicase, Suppressor of ACY-4 sterility 1 (SACY-1). SACY-1 contributed to the longevity of daf-2/insulin/IGF-1 receptor mutants. Unlike HEL-1, SACY-1 was also required for the longevity due to mutations in genes involved in non-IIS pathways. Thus, SACY-1 appears to function as a general longevity factor for various signaling pathways, which is different from the specific function of HEL-1.

Keywords: Aging; C. elegans; HEL-1; RNA helicase; SACY-1; daf-2; insulin/IGF-1 signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans / genetics*
  • Caenorhabditis elegans / physiology*
  • Caenorhabditis elegans Proteins / chemistry
  • Caenorhabditis elegans Proteins / metabolism*
  • DEAD-box RNA Helicases / chemistry
  • DEAD-box RNA Helicases / metabolism*
  • Insulin / metabolism
  • Longevity / genetics*
  • Mutation / genetics
  • Receptor, IGF Type 1 / metabolism
  • Reproduction
  • Signal Transduction
  • Stress, Physiological

Substances

  • Caenorhabditis elegans Proteins
  • Insulin
  • Receptor, IGF Type 1
  • SACY-1 protein, C elegans
  • DEAD-box RNA Helicases