The Human Myt1 Kinase Preferentially Phosphorylates Cdc2 on Threonine 14 and Localizes to the Endoplasmic Reticulum and Golgi Complex

• DOI: 10.1128/mcb.17.2.571
• Publication Date: 2015-10-09T22:06:19Z
• Authors: Feng Liu; Jeffrey J. Stanton; Zhiqi Wu; Helen Piwnica-Worms
• Keywords: 0301 basic medicine; DNA, Complementary; Recombinant Fusion Proteins; Molecular Sequence Data; Golgi Apparatus; Membrane Proteins; Sequence Analysis, DNA; Cyclin B; Protein Serine-Threonine Kinases; Protein-Tyrosine Kinases; Endoplasmic Reticulum; 03 medical and health sciences; Cyclins; CDC2 Protein Kinase; Escherichia coli; Humans; Amino Acid Sequence; RNA, Messenger; Cloning, Molecular; Cyclin B1; Phosphorylation; HeLa Cells

Entry into mitosis requires the activity of Cdc2 kinase. associates with B-type cyclins, and Cdc2-cyclin B heterodimer is in turn regulated by phosphorylation. Phosphorylation threonine 161 required for complex to be catalytically active, whereas phosphorylation 14 tyrosine 15 inhibitory. Human kinases that catalyze have been identified. Here we report isolation a novel human cDNA encoding dual-specificity protein kinase (designated Myt1Hu) preferentially phosphorylates on cyclin-dependent manner. Myt1Hu 46% identical Myt1Xe, recently characterized from Xenopus laevis. localizes endoplasmic reticulum Golgi HeLa cells. A stretch hydrophobic uncharged amino acids located outside catalytic domain likely membrane-targeting domain, as its deletion results localization primarily nucleus.