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.
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Feb 23 2007|
Bibliographical noteFunding 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).
- Mitotic kinesin-like protein 1
- Nuclear localization signal
- Polo-like kinase 1
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology