It is all about the process(ing): P-body granules and the regulation of signal transduction

Curr Genet. 2020 Feb;66(1):73-77. doi: 10.1007/s00294-019-01016-3. Epub 2019 Jul 17.

Abstract

The eukaryotic cell is subdivided into distinct functional domains by the presence of both membrane-bound and membraneless organelles. The latter include cytoplasmic granules, like the Processing-body (P-body), that are induced in response to stress and contain specific sets of mRNAs and proteins. Although P-bodies have been evolutionarily conserved, we do not yet understand the full extent of their biological functions in the cell. Early studies suggested that these structures might be sites of mRNA decay as the first protein constituents identified were enzymes involved in mRNA processing. However, more recent work indicates that this is not likely to be the primary function of these granules and has even suggested that P-bodies are sites of long-term mRNA storage. Interestingly, P-bodies and other ribonucleoprotein granules have been found to also contain a variety of signaling molecules, including protein kinases and phosphatases key to the normal control of cell growth and survival. Therefore, P-bodies could have a role in the modulation of cell signaling during particular types of stress. This review discusses both the general implications of such a proposal and one particular example that illustrates how the granule recruitment of a protein kinase can impact overall cell physiology.

Keywords: Hrr25/CK1 protein kinase; Meiosis; Membraneless organelles; Neurodegenerative disease; Processing-bodies; Signal transduction; mRNA storage.

Publication types

  • Review

MeSH terms

  • Cytoplasmic Granules / metabolism*
  • Eukaryotic Cells / metabolism*
  • Gene Expression Regulation
  • Organelles / metabolism
  • RNA Processing, Post-Transcriptional
  • RNA Stability
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Signal Transduction*
  • Vault Ribonucleoprotein Particles / metabolism

Substances

  • RNA, Messenger
  • Vault Ribonucleoprotein Particles