Dynein at kinetochores: Making the connection.
Dynein removes the checkpoint proteins from kinetochores once chromosomes are bioriented. In this issue, Gama et al. (2017.J. Cell Biol.https://doi.org/10.1083/jcb.201610108) and Mosalaganti et al. (2017.J. Cell Biol.https://doi.org/10.1083/jcb.201611060) reveal the molecular basis for how dynein and its adaptor protein Spindly are recruited to the ROD-Zw10-Zwilch complex in the fibrous corona of unattached kinetochores.
Wellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, Scotland, UK.
Toni
T
McHugh
Wellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, Scotland, UK Julie.welburn@ed.ac.uk.
Julie P I
0000-0002-5440-6060
JP
Welburn
D018797:Cell Cycle Proteins / Q000378:metabolism; D002875:Chromosomes / Q000378:metabolism; D004398:Dyneins / Q000378:metabolism*; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D018386:Kinetochores / Q000378:metabolism*; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism; D008941:Spindle Apparatus / Q000378:metabolism
D018797:Cell Cycle Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins; D004398:Dyneins