The nuclear localization signal of mitotic kinesin-like protein Mklp-1: Effect on Mklp-1 function during cytokinesis

Xiaoqi Liu; Raymond L. Erikson

doi:10.1016/j.bbrc.2006.12.142

The nuclear localization signal of mitotic kinesin-like protein Mklp-1: Effect on Mklp-1 function during cytokinesis

Xiaoqi Liu, Raymond L. Erikson

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

27 Scopus citations

Abstract

The mitotic kinesin-like protein (Mklp-1) localizes in the nucleus during interphase due to the presence of nuclear localization signal(s) [NLS(s)] within its sequence. Here, we mapped two NLSs to be ₈₉₉SRKRRSST₉₀₆ and ₉₄₉KRKKP₉₅₃ in the tail domain of Mklp-1, and showed that ectopic expression of a mutant Mklp-1 without the NLSs leads to cell cycle arrest at cytokinesis, indicating that the NLSs are necessary for Mklp-1 to execute its normal function during cell division. Furthermore, mutation of two serine residues in the first NLS to aspartic acid, which mimics phosphorylation, attenuated its nuclear localization function, suggesting that the function of this NLS might be regulated by phosphorylation.

Original language	English
Pages (from-to)	960-964
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	353
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2006.12.142
State	Published - Feb 23 2007

Bibliographical note

Funding Information:
We thank Eleanor Erikson for critical reading of the manuscript. This work was supported by NIH Grant GM59172. R.L.E. is the John F. Drum American Cancer Society Research Professor. X.L. is a recipient of the Howard Temin Award from the NCI (K01 CA114401).

Keywords

Cytokinesis
Mitotic kinesin-like protein 1
Nuclear localization signal
Phosphorylation
Polo-like kinase 1

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2006.12.142

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title = "The nuclear localization signal of mitotic kinesin-like protein Mklp-1: Effect on Mklp-1 function during cytokinesis",

abstract = "The mitotic kinesin-like protein (Mklp-1) localizes in the nucleus during interphase due to the presence of nuclear localization signal(s) [NLS(s)] within its sequence. Here, we mapped two NLSs to be 899SRKRRSST906 and 949KRKKP953 in the tail domain of Mklp-1, and showed that ectopic expression of a mutant Mklp-1 without the NLSs leads to cell cycle arrest at cytokinesis, indicating that the NLSs are necessary for Mklp-1 to execute its normal function during cell division. Furthermore, mutation of two serine residues in the first NLS to aspartic acid, which mimics phosphorylation, attenuated its nuclear localization function, suggesting that the function of this NLS might be regulated by phosphorylation.",

keywords = "Cytokinesis, Mitotic kinesin-like protein 1, Nuclear localization signal, Phosphorylation, Polo-like kinase 1",

author = "Xiaoqi Liu and Erikson, {Raymond L.}",

note = "Funding Information: We thank Eleanor Erikson for critical reading of the manuscript. This work was supported by NIH Grant GM59172. R.L.E. is the John F. Drum American Cancer Society Research Professor. X.L. is a recipient of the Howard Temin Award from the NCI (K01 CA114401).",

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AU - Liu, Xiaoqi

AU - Erikson, Raymond L.

N1 - Funding Information: We thank Eleanor Erikson for critical reading of the manuscript. This work was supported by NIH Grant GM59172. R.L.E. is the John F. Drum American Cancer Society Research Professor. X.L. is a recipient of the Howard Temin Award from the NCI (K01 CA114401).

PY - 2007/2/23

Y1 - 2007/2/23

N2 - The mitotic kinesin-like protein (Mklp-1) localizes in the nucleus during interphase due to the presence of nuclear localization signal(s) [NLS(s)] within its sequence. Here, we mapped two NLSs to be 899SRKRRSST906 and 949KRKKP953 in the tail domain of Mklp-1, and showed that ectopic expression of a mutant Mklp-1 without the NLSs leads to cell cycle arrest at cytokinesis, indicating that the NLSs are necessary for Mklp-1 to execute its normal function during cell division. Furthermore, mutation of two serine residues in the first NLS to aspartic acid, which mimics phosphorylation, attenuated its nuclear localization function, suggesting that the function of this NLS might be regulated by phosphorylation.

AB - The mitotic kinesin-like protein (Mklp-1) localizes in the nucleus during interphase due to the presence of nuclear localization signal(s) [NLS(s)] within its sequence. Here, we mapped two NLSs to be 899SRKRRSST906 and 949KRKKP953 in the tail domain of Mklp-1, and showed that ectopic expression of a mutant Mklp-1 without the NLSs leads to cell cycle arrest at cytokinesis, indicating that the NLSs are necessary for Mklp-1 to execute its normal function during cell division. Furthermore, mutation of two serine residues in the first NLS to aspartic acid, which mimics phosphorylation, attenuated its nuclear localization function, suggesting that the function of this NLS might be regulated by phosphorylation.

KW - Cytokinesis

KW - Mitotic kinesin-like protein 1

KW - Nuclear localization signal

KW - Phosphorylation

KW - Polo-like kinase 1

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JO - Biochemical and Biophysical Research Communications

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IS - 4

ER -

The nuclear localization signal of mitotic kinesin-like protein Mklp-1: Effect on Mklp-1 function during cytokinesis

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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