Kinesin-4 KIF21B is a potent microtubule pausing factor

Microtubules are dynamic polymers that in cells can grow, shrink or pause, but the factors that promote pausing are poorly understood. Here, we show that the mammalian kinesin-4 KIF21B is a processive motor that can accumulate at microtubule plus ends and induce pausing. A few KIF21B molecules are s...

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Main Authors: Wilhelmina E van Riel, Ankit Rai, Sarah Bianchi, Eugene A Katrukha, Qingyang Liu, Albert JR Heck, Casper C Hoogenraad, Michel O Steinmetz, Lukas C Kapitein, Anna Akhmanova
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2017-03-01
Series:eLife
Subjects:
EB1
Online Access:https://elifesciences.org/articles/24746
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spelling doaj-6f94d5e6bfaf4dc0957d5bb79b6a60082021-05-05T13:19:56ZengeLife Sciences Publications LtdeLife2050-084X2017-03-01610.7554/eLife.24746Kinesin-4 KIF21B is a potent microtubule pausing factorWilhelmina E van Riel0Ankit Rai1https://orcid.org/0000-0002-1569-0919Sarah Bianchi2Eugene A Katrukha3Qingyang Liu4Albert JR Heck5https://orcid.org/0000-0002-2405-4404Casper C Hoogenraad6Michel O Steinmetz7Lukas C Kapitein8https://orcid.org/0000-0001-9418-6739Anna Akhmanova9https://orcid.org/0000-0002-9048-8614Cell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, NetherlandsCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, NetherlandsLaboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen PSI, SwitzerlandCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, NetherlandsCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, NetherlandsBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute for Pharmaceutical Sciences and The Netherlands Proteomics Centre, Utrecht University, Utrecht, NetherlandsCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, NetherlandsLaboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen PSI, SwitzerlandCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, NetherlandsCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, NetherlandsMicrotubules are dynamic polymers that in cells can grow, shrink or pause, but the factors that promote pausing are poorly understood. Here, we show that the mammalian kinesin-4 KIF21B is a processive motor that can accumulate at microtubule plus ends and induce pausing. A few KIF21B molecules are sufficient to induce strong growth inhibition of a microtubule plus end in vitro. This property depends on non-motor microtubule-binding domains located in the stalk region and the C-terminal WD40 domain. The WD40-containing KIF21B tail displays preference for a GTP-type over a GDP-type microtubule lattice and contributes to the interaction of KIF21B with microtubule plus ends. KIF21B also contains a motor-inhibiting domain that does not fully block the interaction of the protein with microtubules, but rather enhances its pause-inducing activity by preventing KIF21B detachment from microtubule tips. Thus, KIF21B combines microtubule-binding and regulatory activities that together constitute an autonomous microtubule pausing factor.https://elifesciences.org/articles/24746microtubule dynamicsKinesinEB1Kinesin-4KIF21Bpausing
collection DOAJ
language English
format Article
sources DOAJ
author Wilhelmina E van Riel
Ankit Rai
Sarah Bianchi
Eugene A Katrukha
Qingyang Liu
Albert JR Heck
Casper C Hoogenraad
Michel O Steinmetz
Lukas C Kapitein
Anna Akhmanova
spellingShingle Wilhelmina E van Riel
Ankit Rai
Sarah Bianchi
Eugene A Katrukha
Qingyang Liu
Albert JR Heck
Casper C Hoogenraad
Michel O Steinmetz
Lukas C Kapitein
Anna Akhmanova
Kinesin-4 KIF21B is a potent microtubule pausing factor
eLife
microtubule dynamics
Kinesin
EB1
Kinesin-4
KIF21B
pausing
author_facet Wilhelmina E van Riel
Ankit Rai
Sarah Bianchi
Eugene A Katrukha
Qingyang Liu
Albert JR Heck
Casper C Hoogenraad
Michel O Steinmetz
Lukas C Kapitein
Anna Akhmanova
author_sort Wilhelmina E van Riel
title Kinesin-4 KIF21B is a potent microtubule pausing factor
title_short Kinesin-4 KIF21B is a potent microtubule pausing factor
title_full Kinesin-4 KIF21B is a potent microtubule pausing factor
title_fullStr Kinesin-4 KIF21B is a potent microtubule pausing factor
title_full_unstemmed Kinesin-4 KIF21B is a potent microtubule pausing factor
title_sort kinesin-4 kif21b is a potent microtubule pausing factor
publisher eLife Sciences Publications Ltd
series eLife
issn 2050-084X
publishDate 2017-03-01
description Microtubules are dynamic polymers that in cells can grow, shrink or pause, but the factors that promote pausing are poorly understood. Here, we show that the mammalian kinesin-4 KIF21B is a processive motor that can accumulate at microtubule plus ends and induce pausing. A few KIF21B molecules are sufficient to induce strong growth inhibition of a microtubule plus end in vitro. This property depends on non-motor microtubule-binding domains located in the stalk region and the C-terminal WD40 domain. The WD40-containing KIF21B tail displays preference for a GTP-type over a GDP-type microtubule lattice and contributes to the interaction of KIF21B with microtubule plus ends. KIF21B also contains a motor-inhibiting domain that does not fully block the interaction of the protein with microtubules, but rather enhances its pause-inducing activity by preventing KIF21B detachment from microtubule tips. Thus, KIF21B combines microtubule-binding and regulatory activities that together constitute an autonomous microtubule pausing factor.
topic microtubule dynamics
Kinesin
EB1
Kinesin-4
KIF21B
pausing
url https://elifesciences.org/articles/24746
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