Article
mik1 and wee1 cooperate in the inhibitory tyrosine phosphorylation of cdc2.
Cell - 22 Mar 1991
Lundgren K, Walworth N, Booher R, Dembski M, Kirschner M, Beach D
Abstract excerpt
wee1 acts antagonistically to cdc25 in the tyrosine dephosphorylation and activation of cdc2, yet biochemical evidence suggests that wee1 is not required for tyrosine phosphorylation and its role is obscure. We show here that a related 66 kd kinase, called mik1, acts redundantly with wee1 in the negative regulation of cdc2 in S. pombe. A null allele of mik1 has no discernible phenotype, but a mik1 wee1 double...
Topics
- Amino Acid Sequence
- Base Sequence
- CDC2 Protein Kinase
- Cloning, Molecular
- Genes, Fungal
- Mitosis
- Molecular Sequence Data
- Mutation
- Phosphorylation
- Phosphotyrosine
- Schizosaccharomyces