Two spatially distinct kinesin-14 proteins, Pkl1 and Klp2, generate collaborative inward forces against kinesin-5 Cut7 in S. pombe

Journal of Cell Science Volume 131 Issue 1 Page jcs210740- published_at 2018-01-04
アクセス数 : 407
ダウンロード数 : 80

今月のアクセス数 : 8
今月のダウンロード数 : 4
File
JCS_131_210740.full.pdf 5.77 MB 種類 : fulltext
Title ( eng )
Two spatially distinct kinesin-14 proteins, Pkl1 and Klp2, generate collaborative inward forces against kinesin-5 Cut7 in S. pombe
Creator
Yamada Yusuke
Yamauchi Tomoaki
Source Title
Journal of Cell Science
Volume 131
Issue 1
Start Page jcs210740
Abstract
Kinesin motors play central roles in bipolar spindle assembly. In many eukaryotes, spindle pole separation is driven by kinesin-5, which generates outward force. This outward force is balanced by antagonistic inward force elicited by kinesin-14 and/or dynein. In fission yeast, two kinesin-14 proteins, Pkl1 and Klp2, play an opposing role against the kinesin-5 motor protein Cut7. However, how the two kinesin-14 proteins coordinate individual activities remains elusive. Here, we show that although deletion of either pkl1 or klp2 rescues temperature-sensitive cut7 mutants, deletion of only pkl1 can bypass the lethality caused by cut7 deletion. Pkl1 is tethered to the spindle pole body, whereas Klp2 is localized along the spindle microtubule. Forced targeting of Klp2 to the spindle pole body, however, compensates for Pkl1 functions, indicating that cellular localizations, rather than individual motor specificities, differentiate between the two kinesin-14 proteins. Interestingly, human kinesin-14 (KIFC1 or HSET) can replace either Pkl1 or Klp2. Moreover, overproduction of HSET induces monopolar spindles, reminiscent of the phenotype of Cut7 inactivation. Taken together, this study has uncovered the biological mechanism whereby two different Kinesin- 14 motor proteins exert their antagonistic roles against kinesin-5 in a spatially distinct manner.
Keywords
Fission yeast
Force generation
Kinesin
Mitotic bipolar spindle
Spindle pole body
Descriptions
This work was supported by the Japan Society for the Promotion of Science (JSPS) [KAKENHI Scientific Research (A) 16H02503 to T.T., a Challenging Exploratory Research grant 16K14672 to T.T., Scientific Research (C) 16K07694 to M.Y.], the Naito Foundation (T.T.) and the Uehara Memorial Foundation (T.T).
Language
eng
Resource Type journal article
Publisher
The Company of Biologists Ltd
Date of Issued 2018-01-04
Rights
© 2018. Published by The Company of Biologists Ltd
Publish Type Version of Record
Access Rights open access
Source Identifier
[ISSN] 0021-9533
[ISSN] 1477-9137
[DOI] 10.1242/jcs.210740
[PMID] 29167352
[DOI] https://doi.org/10.1242/jcs.210740