·     Shapira O., Goldstein A., Al-Bassam J., and Gheber L. "A potential physiological role for bi-directional motility and motor clustering of mitotic kinesin-5 Cin8 in yeast mitosis". Journal of Cell Science 130: 725-734; doi: 10.1242/jcs.195040 (2017)
 
Movie SM1 12x10fp-1-1.m4v
Movie SM1: Motility of Cin8 on immobilized, polarity-marked GMPCPP-stabilized MTs.
Cin8 undergoes fast minus-end–directed motility and clusters at the minus-end of the MTs. Clusters of Cin8 undergo slow plus-end–directed motility. Left: immobilized GMPCPP-stabilized red MTs, yellow labels the MT plus-end; Right: Cin8. Bar: 10 μm. Time interval between frames: 1.28 s. Movie sped up 12.8X, 10 fps.
 
  • Movie SM3: Cin8 tracks the minus-end of dynamic MTs.
    MTs#1 and #2: Cin8 tracks the MT minus-end. Yellow: GMPCPP-stabilized seeds; Red: dynamic MTs; White: Cin8. Plus- and minus-ends of MTs are indicated, based on the difference in dynamics at the two ends. Bar: 5 μm. Time intervals between frames: 3.3 s. Movie sped up 30X, 9 fps.
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  • Movie SM4: Plus-end–directed Cin8 cluster, moving on a dynamic MT, splits into several clusters, some of which are moving in the minus-end direction of the MT.
  • Movie relates to Fig. 2E, upper left panel. Only Cin8 (GFP channel) is shown, the directionality of the MT is indicated based on the different dynamics of the plus- and minus-ends. Arrowheads mark the location of clusters; change in the arrowhead color indicates a cluster-splitting event. Bar: 3 μm. Time intervals between frames: 3.4 s. Movie sped up 34X, 10 fps.
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  • Movie SM5: Cin8 cluster-mediated antiparallel MT capturing and subsequent sliding.
  • Red MT with yellow label of the plus-end is immobilized to the glass surface. Yellow MTs with red label of the plus-end are free in solution. The different channels are indicated. Cin8 cluster that is bound to the minus-end of the red MT mediates the capturing and subsequent antiparallel sliding of the yellow MT. Bar: 2 μm. Time interval between frames: 3.7 s. Movie sped up 30X, 8 fps.
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Movie SM7: MT capturing and pivoting during antiparallel sliding, mediated by a cluster located at the minus-end of the immobilized (red) MT.
Red MTs are immobilized to the glass surface, yellow MTs are free in solution; Cin8 is shown in white. Left panel: immobilized and free MTs and Cin8; right panel: immobilized MTs and Cin8. The yellow MT undergoes antiparallel sliding, mediated by a cluster of Cin8 located at the minus-end of the red MT. The yellow MT pivots around the minus-end located Cin8 cluster. Minus- and plus end of the red MT are indicated based on the location of the Cin8 cluster. Bar: 5 μm. Time interval between frames: 3.6 s. Movie sped up 36X, 10 fps.
 
 
·    Shapira O. and Gheber L. (2016), "Motile properties of the bidirectional kinesin-5 Cin8 are affected by phosphorylation in its motor domain", Scientific Reports 6; doi:10.1038/srep25597 (2016)
 
Supplementary Movie S7: Purified sample of wt Cin8 in MB buffer supplemented with 45 mM NaCl and 4 mM ATP. MT labeled with low ratio of rhodamine-tubulin is in red. MT seed, which marks the MT minus-end and undergoes photobleaching during the movie, is labeled with Atto488-tubulin (on the left, seen in green). Cin8-3GFP molecules are in green. The original frame rate is 1 frame/s, the movie is expedited 18X. 
Supplementary Movie S8: Purified sample of Cin8-3D in MB buffer supplemented with 45 mM NaCl and 4 mM ATP. MT labeled with low ratio of rhodamine-tubulin is in red. MT seed, which marks the MT minus-end, is labeled with Atto488-tubulin (on the left, seen in green). Cin8-3GFP molecules are in green. The original frame rate is 1 frame/s, the movie is expedited 18X.
 
Supplementary Movie S9: Purified sample of wt Cin8 in MB buffer supplemented with 135 mM NaCl and 4 mM ATP. MT labeled with low ratio of rhodamine-tubulin is in red. MT seed, which marks the MT minus-end and undergoes photobleaching during the movie, is labeled with Atto488-tubulin (on the left, seen in green). Cin8-3GFP molecules are in green. The original frame rate is 1 frame/s, the movie is expedited 18X.