Signaling pathways regulating protein synthesis during ageing

Exp Gerontol. 2006 Oct;41(10):1020-5. doi: 10.1016/j.exger.2006.05.014. Epub 2006 Jul 7.

Abstract

Ageing in many organisms, including humans, is accompanied by marked alterations in both general and specific protein synthesis. Protein synthesis is normally under tight control by a broad array of regulatory factors, which facilitate appropriate rates of mRNA translation. Are the wide changes in protein synthesis simply a corollary of the ageing process or do they have a causative role in senescent decline? The jury is still out on this important question. Nevertheless, recent studies reveal an intimate interface between mechanisms that govern the translation of mRNA and molecular pathways implicated in ageing. In our manuscript we consider these links, which potentially underlie age-associated changes in protein synthesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Aging / genetics
  • Aging / physiology*
  • Animals
  • Caenorhabditis elegans / metabolism
  • Caenorhabditis elegans Proteins / metabolism
  • Cytoplasm / metabolism
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / metabolism
  • Humans
  • Insulin / metabolism
  • Insulin-Like Growth Factor I / metabolism
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Protein Biosynthesis / genetics
  • Protein Biosynthesis / physiology*
  • Protein Kinases / metabolism
  • Protein Serine-Threonine Kinases
  • RNA, Messenger / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / metabolism
  • Signal Transduction / genetics
  • Signal Transduction / physiology*
  • TOR Serine-Threonine Kinases

Substances

  • Caenorhabditis elegans Proteins
  • Drosophila Proteins
  • Insulin
  • RNA, Messenger
  • Saccharomyces cerevisiae Proteins
  • Insulin-Like Growth Factor I
  • Protein Kinases
  • Phosphotransferases (Alcohol Group Acceptor)
  • let-363 protein, C elegans
  • target of rapamycin protein, Drosophila
  • Protein Serine-Threonine Kinases
  • TOR Serine-Threonine Kinases
  • target of rapamycin protein, S cerevisiae