Self-association of coilin reveals a common theme in nuclear body localization

Mol Biol Cell. 2000 Dec;11(12):4159-71. doi: 10.1091/mbc.11.12.4159.

Abstract

We have found that coilin, the marker protein for Cajal bodies (coiled bodies, CBs), is a self-interacting protein, and we have mapped the domain responsible for this activity to the amino-terminus. Together with a nuclear localization signal, the self-interaction domain is necessary and sufficient for localization to CBs. Overexpression of various wild-type and mutant coilin constructs in HeLa cells results in disruption of both CBs and survival motor neurons (SMN) gems. Additionally, we have identified a cryptic nucleolar localization signal (NoLS), within the coilin protein, which may be exposed in specific coilin phospho-isoforms. The implications of these findings are discussed in light of the fact that other proteins known to localize within nuclear bodies (e. g., PML, SMN and Sam68) can also self-associate. Thus protein self-interaction appears to be a general feature of nuclear body marker proteins.

Publication types

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

MeSH terms

  • Cell Nucleolus / metabolism
  • Coiled Bodies / metabolism*
  • DNA Mutational Analysis
  • HeLa Cells
  • Humans
  • Mutation
  • Nuclear Localization Signals
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Phosphorylation
  • Phosphoserine / metabolism
  • Transfection

Substances

  • Nuclear Localization Signals
  • Nuclear Proteins
  • p80-coilin
  • Phosphoserine