4.7 Article

Opposing kinesin complexes queue at plus tips to ensure microtubule catastrophe at cell ends

期刊

EMBO REPORTS
卷 19, 期 11, 页码 -

出版社

WILEY
DOI: 10.15252/embr.201846196

关键词

cytoskeleton; fission yeast; kinesin; microtubules

资金

  1. Medical Research Council UK programme grant [MR/K001000/1]
  2. Wellcome Trust Senior Investigator Awards [103895/Z/14/Z, WT101885MA]
  3. ERC Advanced Grant (Actomyosin Ring-ERC-2014-ADG) [671083]
  4. Royal Society Wolfson Merit Award [WM130042]
  5. University of Warwick, Institute of Advanced Study, Global Research Fellowship
  6. University of Warwick
  7. Medical Research Council UK
  8. European Research Council (ERC) [671083] Funding Source: European Research Council (ERC)
  9. MRC [MR/K001000/1] Funding Source: UKRI
  10. Wellcome Trust [103895/Z/14/Z] Funding Source: Wellcome Trust

向作者/读者索取更多资源

In fission yeast, the lengths of interphase microtubule (iMT) arrays are adapted to cell length to maintain cell polarity and to help centre the nucleus and cell division ring. Here, we show that length regulation of iMTs is dictated by spatially regulated competition between MT-stabilising Tea2/Tip1/Mal3 (Kinesin-7) and MT-destabilising Klp5/Klp6/Mcp1 (Kinesin-8) complexes at iMT plus ends. During MT growth, the Tea2/Tip1/Mal3 complex remains bound to the plus ends of iMT bundles, thereby restricting access to the plus ends by Klp5/Klp6/Mcp1, which accumulate behind it. At cell ends, Klp5/Klp6/Mcp1 invades the space occupied by the Tea2/Tip1/Tea1 kinesin complex triggering its displacement from iMT plus ends and MT catastrophe. These data show that in vivo, whilst an iMT length-dependent model for catastrophe factor accumulation has validity, length control of iMTs is an emergent property reflecting spatially regulated competition between distinct kinesin complexes at the MT plus tip.

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