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 journalArticlepeer-review

26 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 languageEnglish
Pages (from-to)960-964
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume353
Issue number4
DOIs
StatePublished - 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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