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Opposing kinesin complexes queue at plus tips to ensure microtubule catastrophe at cell ends
Author(s) -
Meadows John C,
Messin Liam J,
Kamnev Anton,
Lancaster Theresa C,
Balasubramanian Mohan K,
Cross Robert A,
Millar Jonathan BA
Publication year - 2018
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201846196
Subject(s) - kinesin , microtubule , microbiology and biotechnology , queue , biophysics , physics , biology , chemistry , computer science , computer network
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 iMT s 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 iMT s is an emergent property reflecting spatially regulated competition between distinct kinesin complexes at the MT plus tip.