A bipolar kinesin

A. S. Kashina; R. J. Baskin; D. G. Cole; K. P. Wedaman; W. M. Saxton; J. M. Scholey

doi:10.1038/379270a0

A bipolar kinesin

A. S. Kashina, R. J. Baskin, D. G. Cole, K. P. Wedaman, W. M. Saxton, J. M. Scholey

Molecular and Cellular Biology

Research output: Contribution to journal › Article

262 Scopus citations

Abstract

CHROMOSOME segregation during mitosis depends on the action of the mitotic spindle, a self organizing, bipolar protein machine which uses microtubules (MTs) and their associated motors. Members of the BimC subfamily of kinesin related MT-motor proteins are believed to be essential for the formation and functioning of a normal bipolar spindle. Here we report that KRP₁₃₀, a homotetrameric BimC-related kinesin purified from Drosophila melanogaster embryos, has an unusual ultrastructure. It consists of four kinesin-related polypeptides assembled into a bipolar aggregate with motor domains at opposite ends, analogous to a miniature myosin filament. Such a bipolar 'minifilament' could crosslink spindle MTs and slide them relative to one another. We do not know of any other MT motors that have a bipolar structure.

Original language	English (US)
Pages (from-to)	270-272
Number of pages	3
Journal	Nature
Volume	379
Issue number	6562
DOIs	https://doi.org/10.1038/379270a0
State	Published - Jan 18 1996

Fingerprint

ASJC Scopus subject areas

General

Cite this

Kashina, A. S., Baskin, R. J., Cole, D. G., Wedaman, K. P., Saxton, W. M., & Scholey, J. M. (1996). A bipolar kinesin. Nature, 379(6562), 270-272. https://doi.org/10.1038/379270a0

@article{c228722824684dd49bc61e20c212ab97,

title = "A bipolar kinesin",

abstract = "CHROMOSOME segregation during mitosis depends on the action of the mitotic spindle, a self organizing, bipolar protein machine which uses microtubules (MTs) and their associated motors. Members of the BimC subfamily of kinesin related MT-motor proteins are believed to be essential for the formation and functioning of a normal bipolar spindle. Here we report that KRP130, a homotetrameric BimC-related kinesin purified from Drosophila melanogaster embryos, has an unusual ultrastructure. It consists of four kinesin-related polypeptides assembled into a bipolar aggregate with motor domains at opposite ends, analogous to a miniature myosin filament. Such a bipolar 'minifilament' could crosslink spindle MTs and slide them relative to one another. We do not know of any other MT motors that have a bipolar structure.",

author = "Kashina, {A. S.} and Baskin, {R. J.} and Cole, {D. G.} and Wedaman, {K. P.} and Saxton, {W. M.} and Scholey, {J. M.}",

year = "1996",

month = jan

day = "18",

doi = "10.1038/379270a0",

language = "English (US)",

volume = "379",

pages = "270--272",

journal = "Nature",

issn = "0028-0836",

publisher = "Nature Publishing Group",

number = "6562",

}

TY - JOUR

T1 - A bipolar kinesin

AU - Kashina, A. S.

AU - Baskin, R. J.

AU - Cole, D. G.

AU - Wedaman, K. P.

AU - Saxton, W. M.

AU - Scholey, J. M.

PY - 1996/1/18

Y1 - 1996/1/18

N2 - CHROMOSOME segregation during mitosis depends on the action of the mitotic spindle, a self organizing, bipolar protein machine which uses microtubules (MTs) and their associated motors. Members of the BimC subfamily of kinesin related MT-motor proteins are believed to be essential for the formation and functioning of a normal bipolar spindle. Here we report that KRP130, a homotetrameric BimC-related kinesin purified from Drosophila melanogaster embryos, has an unusual ultrastructure. It consists of four kinesin-related polypeptides assembled into a bipolar aggregate with motor domains at opposite ends, analogous to a miniature myosin filament. Such a bipolar 'minifilament' could crosslink spindle MTs and slide them relative to one another. We do not know of any other MT motors that have a bipolar structure.

AB - CHROMOSOME segregation during mitosis depends on the action of the mitotic spindle, a self organizing, bipolar protein machine which uses microtubules (MTs) and their associated motors. Members of the BimC subfamily of kinesin related MT-motor proteins are believed to be essential for the formation and functioning of a normal bipolar spindle. Here we report that KRP130, a homotetrameric BimC-related kinesin purified from Drosophila melanogaster embryos, has an unusual ultrastructure. It consists of four kinesin-related polypeptides assembled into a bipolar aggregate with motor domains at opposite ends, analogous to a miniature myosin filament. Such a bipolar 'minifilament' could crosslink spindle MTs and slide them relative to one another. We do not know of any other MT motors that have a bipolar structure.

UR - http://www.scopus.com/inward/record.url?scp=0030025443&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030025443&partnerID=8YFLogxK

U2 - 10.1038/379270a0

DO - 10.1038/379270a0

M3 - Article

C2 - 8538794

AN - SCOPUS:0030025443

VL - 379

SP - 270

EP - 272

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6562

ER -

Access to Document

10.1038/379270a0