Coilin methylation regulates nuclear body formation

Dev Cell. 2002 Sep;3(3):329-37. doi: 10.1016/s1534-5807(02)00222-8.

Abstract

Cajal bodies (CBs) are nuclear suborganelles involved in biogenesis of small RNAs. Twin structures, called gems, contain high concentrations of the survival motor neurons (SMN) protein complex. CBs and gems often colocalize, and communication between these subdomains is mediated by coilin, the CB marker. Coilin contains symmetrical dimethylarginines that modulate its affinity for SMN, and, thus, localization of SMN complexes to CBs. Inhibition of methylation or mutation of the coilin RG box dramatically decreases binding of coilin to SMN, resulting in gem formation. Coilin is hypomethylated in cells that display gems, but not in those that primarily contain CBs. Likewise, extracts prepared from cells that display gems are less efficient in methylating coilin and Sm constructs in vitro. These results demonstrate that alterations in protein methylation status can affect nuclear organization.

Publication types

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

MeSH terms

  • Adenosine / analogs & derivatives
  • Adenosine / pharmacology
  • Amino Acid Sequence
  • Animals
  • Arginine / analogs & derivatives
  • Arginine / biosynthesis
  • Arginine / metabolism
  • Cell Line
  • Cell Nucleus / metabolism
  • Cells, Cultured
  • Coiled Bodies / metabolism*
  • Cyclic AMP Response Element-Binding Protein
  • Enzyme Inhibitors / pharmacology
  • Fibroblasts / cytology
  • Fibroblasts / metabolism
  • Gene Deletion
  • Green Fluorescent Proteins
  • HeLa Cells
  • Humans
  • Luminescent Proteins / metabolism
  • Methylation
  • Mice
  • Molecular Sequence Data
  • Mutation
  • Nerve Tissue Proteins / metabolism
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / physiology*
  • Peptides / chemistry
  • Peptides / metabolism
  • Protein-Arginine N-Methyltransferases / antagonists & inhibitors
  • Protein-Arginine N-Methyltransferases / metabolism
  • RNA-Binding Proteins
  • SMN Complex Proteins
  • Transfection
  • Tumor Cells, Cultured

Substances

  • Cyclic AMP Response Element-Binding Protein
  • Enzyme Inhibitors
  • Luminescent Proteins
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Peptides
  • RNA-Binding Proteins
  • SMN Complex Proteins
  • p80-coilin
  • Green Fluorescent Proteins
  • Arginine
  • Protein-Arginine N-Methyltransferases
  • Adenosine