Subcellular localisation of human wee1 kinase is regulated during the cell cycle.
Wee1 kinase-dependent phosphorylation of cdc2 maintains the cdc2/cyclin B complex in an inert form until it is activated by the cdc25 tyrosine phosphatase at the end of G2. As described for cdc25, cell cycle-linked changes in the intracellular localisation of wee1 may constitute an important aspect of the temporal regulation of cdc2 activity. Here we report that the subcellular distribution of human wee1 changes during the cell cycle in HeLa and IMR90 cells. During interphase, wee1 is found almost exclusively in the nucleus. When the cell enters mitosis, wee1 is relocalised into the cytoplasm. During cell division, wee1 becomes restricted to the mitotic equator and by the end of mitosis it is found exclusively in association with midbody bridges, a phenomenon that is dependent on microtubule assembly. The relocalisations of wee1 and its association with subcellular structures may play key regulatory roles at different stages of the cell cycle and during mitosis.
Baldin
V
V
Laboratoire de Pharmacologie, CNRS, Université Paul Sabatier, Toulouse, France.
Ducommun
B
B
D001692:Biological Transport; D002451:Cell Compartmentation; D002453:Cell Cycle / Q000502:physiology*; D018797:Cell Cycle Proteins; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006801:Humans; D008870:Microtubules / Q000502:physiology; D009687:Nuclear Proteins; D011505:Protein-Tyrosine Kinases / Q000096:biosynthesis*
D018797:Cell Cycle Proteins; D009687:Nuclear Proteins; D011505:Protein-Tyrosine Kinases; C499349:WEE1 protein, human