High impact information on VIK1

• Kinesin kar3 and vik1 go head to head [1].
• However, this does not hinder movement of the heterodimer because other features of the remarkably divergent Vik1 motor domain are retained, including the ability to bind microtubules [1].
• Vik1 Modulates Microtubule-Kar3 Interactions through a Motor Domain that Lacks an Active Site [2].
• We have identified a Saccharomyces cerevisiae gene, named VIK1, encoding a protein with sequence and structural similarity to Cik1p [3].
• This loss in viability is partially attributable to vegetative chromosome loss in vik1 diploids [4].

Biological context of VIK1

• These data are consistent with the model that Cik1p is necessary for some, but not all, of the roles of Kar3p in meiosis I. vik1 mutants sporulate at wild-type levels, but have reduced spore viability [4].
• Cik1p and Vik1p are kinesin-associated proteins known to modulate the function of Kar3p in the microtubule-dependent processes of karyogamy and mitosis [4].

Anatomical context of VIK1

• Disruption of VIK1 causes increased resistance to the microtubule depolymerizing drug benomyl and partially suppresses growth defects of cik1Delta mutants [3].

Other interactions of VIK1

• Vik1p localizes to the spindle-pole body region in a Kar3p-dependent manner [3].

References