High impact information on KIP2

• This movement is dependent upon the microtubule motor protein Kip2 [1].
• The observation that deletion of KIP2 could also suppress the inviability of dyn1Delta kar3Delta cells suggests that kinesin-related Kar3p also contributes to spindle positioning [2].
• Likewise, induced expression of KIP2 caused spindles to mislocalize in cells deficient for dynein and Kip3p [2].
• Most significantly, the deletion of KIP2 greatly suppressed the spindle localization defect and slow growth exhibited by dyn1 kip3 cells [2].
• We identified two new Saccharomyces cerevisiae kinesin-related genes, KIP1 and KIP2, using polymerase chain reaction primers corresponding to highly conserved regions of the kinesin motor domain [3].

Biological context of KIP2

• Localization studies found Kip2p exclusively on cytoplasmic microtubules throughout the cell cycle, whereas GFP-Kip3p localized to both spindle and cytoplasmic microtubules [4].
• Loss of both the Kip2p and Kar3p motors together in the same cell produces an intermediate phenotype, suggesting that these two motors act in opposition to control cytoplasmic microtubule density [5].
• A Kip2p-GFP fusion from single gene expression is most concentrated at the spindle poles, as shown previously for an epitope tagged Kar3p-HA, suggesting both of these motors act from the minus ends of the microtubules to influence microtubule numbers [5].

Anatomical context of KIP2

• Others operate on the cytoplasmic microtubules to effect spindle and nuclear positioning within the cell (dynein and kinesin-related Kip2p, Kip3p and Kar3p) [6].

Physical interactions of KIP2

• Bik1 forms a complex with the kinesin Kip2 [7].

Other interactions of KIP2

• Our findings indicate that Kip2p participates in normal spindle positioning but antagonizes a positioning mechanism acting in dyn1 kip3 cells [2].
• As with Bik1, the targeting of dynein to the microtubule plus end requires Kip2 [7].

References