Mutations in the ATP-binding domain affect the subcellular distribution of mitotic centromere-associated kinesin (MCAK)

Cell Biol Int. 1999;23(4):275-86. doi: 10.1006/cbir.1999.0359.

Abstract

Mitotic centromere-associated kinesin (MCAK) is important for anaphase chromosome segregation. MCAK is diffusely localized to both the cytoplasm and the nucleus during interphase. At prophase MCAK is recruited to mitotic centromeres. It is associated with centromeres throughout mitosis and then returns to exhibiting a diffuse nuclear and cytoplasmic localization during interphase. MCAK has several predicted nuclear localization sequences. The subcellular distribution of expressed deletion constructs of GFP-MCAK suggest that the nucleocytoplasmic ratio of MCAK protein is dependent on a balance between several predicted nuclear localization sequences (NLS) and a putative nuclear exclusion sequence (NES) in the amino-terminal region of MCAK. Amino acid substitutions in the ATP-binding domain of the MCAK motor affect nuclear localization, which, in turn, influences the degree of centromere binding.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Anaphase / physiology
  • Animals
  • Binding Sites
  • CHO Cells / chemistry
  • Cell Nucleus / metabolism
  • Cells, Cultured
  • Centromere / physiology
  • Cricetinae
  • Cytoplasm / metabolism
  • Green Fluorescent Proteins
  • Humans
  • Interphase / physiology
  • Kinesins / metabolism*
  • Luminescent Proteins / metabolism
  • Mice
  • Middle Aged
  • Mitosis
  • Molecular Sequence Data
  • Mutation
  • Rats
  • Recombinant Proteins / metabolism
  • Sequence Alignment

Substances

  • KIF2C protein, human
  • Luminescent Proteins
  • Recombinant Proteins
  • mitotic centromere-associated kinesin, hamster
  • Green Fluorescent Proteins
  • Adenosine Triphosphate
  • Kinesins