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MUTATIONS IN THE ATP‐BINDING DOMAIN AFFECT THE SUBCELLULAR DISTRIBUTION OF MITOTIC CENTROMERE‐ASSOCIATED KINESIN (MCAK)
Author(s) -
Wordeman Linda,
Wagenbach Mike,
Maney Todd
Publication year - 1999
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1999.0359
Subject(s) - centromere , kinesin , mitosis , anaphase , microbiology and biotechnology , interphase , biology , chromosome segregation , prophase , cytoplasm , microtubule , genetics , chromosome , meiosis , gene
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 subcelluar 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.