Response to Zambon et al.
Stimulated by our 2015 Current Biology paper [1], Zambon et al. reinvestigated how three myosin isoforms participate in the formation and constriction of the contractile ring in fission yeast. Our paper presented evidence that these myosin isoforms have distinct roles: "Conventional myosin-II Myo2 is crucial to ring assembly, unconventional myosin-II Myp2 is most important for ring constriction, and type V myosin Myo51 aids the other two myosins." Zambon et al. used different markers to reexamine the contributions of the three myosins to cytokinesis and concluded "that Myo2p is the major motor involved in ring contraction in S. pombe." Here, we show that most of the differences observed by Zambon et al. can be attributed to their use of the Rlc1p-3GFP marker, which genetically interacts with myo2-E1.
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
Caroline
C
Laplante
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA; Department of Cell Biology, Yale University, New Haven, CT 06520, USA. Electronic address: thomas.pollard@yale.edu.
Thomas D
TD
Pollard
D003250:Constriction; D018995:Myosin Heavy Chains; D024462:Myosin Type II; D009218:Myosins; D012568:Schizosaccharomyces; D029702:Schizosaccharomyces pombe Proteins
C434211:MYO2 protein, S pombe; C110514:Myp2 protein, S pombe; D029702:Schizosaccharomyces pombe Proteins; D024462:Myosin Type II; C554096:Myo51 protein, S pombe; D018995:Myosin Heavy Chains; D009218:Myosins