Kinesin is associated with a nonmicrotubule component of sea urchin mitotic spindles.

R. J. Leslie; R. B. Hird; L. Wilson; J. R. McIntosh; J. M. Scholey

Kinesin is associated with a nonmicrotubule component of sea urchin mitotic spindles.

R. J. Leslie, R. B. Hird, L. Wilson, J. R. McIntosh, J. M. Scholey

Research output: Contribution to journal › Article › peer-review

Abstract

Sea urchin embryos in second division have been lysed into microtubule-stabilizing buffers to yield mitotic cytoskeletons (MCSs) that consist of two mitotic spindles surrounded by a cortical array of filaments. Microtubules have been completely extracted from MCSs by incubation at 0 degrees C with Ca2+-containing buffer. An antibody to the microtubule translocator kinesin stains the spindles in MCSs and in MCSs treated with 5 mM ATP and also stains spindle-remnants of the MCSs after the microtubules have been extracted. We conclude that kinesin binds to a nonmicrotubule component in the mitotic spindle. Based on these results, we present several models of kinesin function in the spindle.

Original language	English (US)
Pages (from-to)	2771-2775
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	84
Issue number	9
State	Published - May 1987
Externally published	Yes

ASJC Scopus subject areas

General
Genetics

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title = "Kinesin is associated with a nonmicrotubule component of sea urchin mitotic spindles.",

abstract = "Sea urchin embryos in second division have been lysed into microtubule-stabilizing buffers to yield mitotic cytoskeletons (MCSs) that consist of two mitotic spindles surrounded by a cortical array of filaments. Microtubules have been completely extracted from MCSs by incubation at 0 degrees C with Ca2+-containing buffer. An antibody to the microtubule translocator kinesin stains the spindles in MCSs and in MCSs treated with 5 mM ATP and also stains spindle-remnants of the MCSs after the microtubules have been extracted. We conclude that kinesin binds to a nonmicrotubule component in the mitotic spindle. Based on these results, we present several models of kinesin function in the spindle.",

author = "Leslie, {R. J.} and Hird, {R. B.} and L. Wilson and McIntosh, {J. R.} and Scholey, {J. M.}",

year = "1987",

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journal = "Proceedings of the National Academy of Sciences of the United States of America",

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T1 - Kinesin is associated with a nonmicrotubule component of sea urchin mitotic spindles.

AU - Leslie, R. J.

AU - Hird, R. B.

AU - Wilson, L.

AU - McIntosh, J. R.

AU - Scholey, J. M.

PY - 1987/5

Y1 - 1987/5

N2 - Sea urchin embryos in second division have been lysed into microtubule-stabilizing buffers to yield mitotic cytoskeletons (MCSs) that consist of two mitotic spindles surrounded by a cortical array of filaments. Microtubules have been completely extracted from MCSs by incubation at 0 degrees C with Ca2+-containing buffer. An antibody to the microtubule translocator kinesin stains the spindles in MCSs and in MCSs treated with 5 mM ATP and also stains spindle-remnants of the MCSs after the microtubules have been extracted. We conclude that kinesin binds to a nonmicrotubule component in the mitotic spindle. Based on these results, we present several models of kinesin function in the spindle.

AB - Sea urchin embryos in second division have been lysed into microtubule-stabilizing buffers to yield mitotic cytoskeletons (MCSs) that consist of two mitotic spindles surrounded by a cortical array of filaments. Microtubules have been completely extracted from MCSs by incubation at 0 degrees C with Ca2+-containing buffer. An antibody to the microtubule translocator kinesin stains the spindles in MCSs and in MCSs treated with 5 mM ATP and also stains spindle-remnants of the MCSs after the microtubules have been extracted. We conclude that kinesin binds to a nonmicrotubule component in the mitotic spindle. Based on these results, we present several models of kinesin function in the spindle.

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