Regulation of Nek6 Functions by Its SUMOylation on the $K^{252}$ Residue

Nek6 belongs to NIMA1 (never in mitosis, gene A) related kinase, which was originally identified in Aspergillus nidulans as a serine/threonine kinase critical for cell cycle progression. We noticed that the putative SUMOylation site is localized on the $K^{252}$ residue in $^{251}FKsD^{254}$ of Nek6...

Full description

Saved in:
Bibliographic Details
Published in:Integrative biosciences 2007, Vol.11 (2), p.205-213
Main Authors: Lee, Eun-Jeoung, Hyun, Sung-Hee, Chun, Jae-Sun, Shin, Sung-Hwa, Lee, Kyung-Eun, Park, In-Suk, Kang, Sang-Sun
Format: Article
Language:Korean
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Nek6 belongs to NIMA1 (never in mitosis, gene A) related kinase, which was originally identified in Aspergillus nidulans as a serine/threonine kinase critical for cell cycle progression. We noticed that the putative SUMOylation site is localized on the $K^{252}$ residue in $^{251}FKsD^{254}$ of Nek6, based on the consensus sequence ${\Phi}KxE$; where ${\Phi}$ represents L, I, V or F and x is any amino acid. We observed that the Nek6 SUMO mutant (K252R) has decreased protein kinase activity, nuclear speckle localization and protein stability, compared with that of the Nek6 wild type. However, the Nek6 SUMO mutant increased the cell survival rate of COS-1 cells as determined by FACS analysis. Therefore, our data suggest that SUMOylation on the $K^{252}$ residue of Nek6 is required for its normal functions, such as proper nuclear localization, kinase activity and protein stability, to control cell cycle.
ISSN:1738-6357
1738-7078