English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

The human kinesin-14 HSET tracks the tips of growing microtubules in vitro.

MPS-Authors
/persons/resource/persons219036

Braun,  Marcus
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219371

Lansky,  Zdenek
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219155

Fink,  Gero
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219112

Diez,  Stefan
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Braun, M., Lansky, Z., Bajer, S., Fink, G., Kasprzak, A. A., & Diez, S. (2013). The human kinesin-14 HSET tracks the tips of growing microtubules in vitro. Cytoskeleton (Hoboken, N.J.), 70(9), 515-521.


Cite as: https://hdl.handle.net/21.11116/0000-0001-0768-3
Abstract
Tip-tracking of kinesin-14 motor proteins is believed to be crucial for the assembly and maintenance of dynamic microtubule arrays. However, in contrast to other members of the kinesin-14 family, H. sapiens kinesin-14 HSET has so far never been observed to be prominently located at microtubule plus ends. Here, using an in vitro microtubule dynamics reconstitution assay we observe tip-tracking of GFP-HSET in the presence of H. sapiens EB1 (hsEB1). Tip-tracking depended on the SxIP-like motif in HSET as well as on the EB homology domain in hsEB1. D. melanogaster Ncd and S. pombe Klp2 tip-tracking reconstitution assays accompanied by kinesin-14 amino acid sequence comparisons suggest that SxIP-like motif mediated tip-tracking dependent on EB family proteins is conserved in the kinesin-14 family of molecular motors.