ArticleThe Journal of cell biology1998
Smy1p, a kinesin-related protein that does not require microtubules.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- The Orphan Kinesin PAKRP2 Achieves Processive Motility via a Noncanonical Stepping Mechanism.Biophysical journal · 2019Article
- Kinesin-related Smy1 enhances the Rab-dependent association of myosin-V with secretory cargo.Molecular biology of the cell · 2016Article
- Common formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo.Molecular biology of the cell · 2016Article
- Article
- Phylogenetic analysis of the Kinesin superfamily from physcomitrella.Frontiers in plant science · 2012Article
- Phosphorylation of Kif26b promotes its polyubiquitination and subsequent proteasomal degradation during kidney development.PloS one · 2012Article
- The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper.Developmental cell · 2011Article
- Phosphorylation provides a negative mode of regulation for the yeast Rab GTPase Sec4p.PloS one · 2011Article
- Why have chloroplasts developed a unique motility system?Plant signaling & behavior · 2010Review
- Two kinesin-like proteins mediate actin-based chloroplast movement in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- A nonprocessive class V myosin drives cargo processively when a kinesin- related protein is a passenger.Current biology : CB · 2009Article
- Dosage rescue by UBC4 restores cell wall integrity in Saccharomyces cerevisiae lacking the myosin type II gene MYO1.Yeast (Chichester, England) · 2007Article
- Slip sliding away with myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Comprehensive comparative analysis of kinesins in photosynthetic eukaryotes.BMC genomics · 2006Article
- Myosin-V, Kinesin-1, and Kinesin-3 cooperate in hyphal growth of the fungus Ustilago maydis.Molecular biology of the cell · 2005Article
- Cytokinesis depends on the motor domains of myosin-II in fission yeast but not in budding yeast.Molecular biology of the cell · 2005Article
- Meiotic telomere clustering requires actin for its formation and cohesin for its resolution.The Journal of cell biology · 2005Article
- dsu functions in a MYO5A-independent pathway to suppress the coat color of dilute mice.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Polarized growth and organelle segregation in yeast: the tracks, motors, and receptors.The Journal of cell biology · 2003Review
- Orphan kinesin NOD lacks motile properties but does possess a microtubule-stimulated ATPase activity.Molecular biology of the cell · 2001Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We have previously reported that a defect in Myo2p, a myosin in budding yeast (Saccharomyces cerevisiae), can be partially corrected by overexpression of Smy1p, which is by sequence a kinesin-related protein (Lillie, S.H., and S.S. Brown. 1992. Nature. 356:358- 361). Such a functional link between putative actin- and microtubule-based motors is surprising, so here we have tested the prediction that Smy1p indeed acts as a microtubule-based motor. Unexpectedly, we found that abolition of microtubules by nocodazole does not interfere with the ability of Smy1p to correct the mutant Myo2p defect, nor does it interfere with the ability of Smy1p to localize properly. In addition, other perturbations of microtubules, such as treatment with benomyl or introduction of tubulin mutations, do not exacerbate the Myo2p defect. Furthermore, a mutation in SMY1 strongly predicted to destroy motor activity does not destroy Smy1p function. We have also observed a genetic interaction between SMY1 and two of the late SEC mutations, sec2 and sec4. This indicates that Smy1p can play a role even when Myo2p is wild type, and that Smy1p acts at a specific step of the late secretory pathway. We conclude that Smy1p does not act as a microtubule-based motor to localize properly or to compensate for defective Myo2p, but that it must instead act in some novel way.
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