Deciliation Induces Phosphorylation of a 90‐kDa Cortical Protein in Tetrahymena thermophila

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Abstract
We have used the anti‐phosphoprotein antibody MPM‐2 to examine changes in phosphorytation of cortical proteins during cilia regeneration in Tetrahymena thermophila. Although numerous cortical proteins are phosphorylated in both nondeciliated and deciliated cells, deciliation induces a dramatic increase in the phosphorylation of a 90‐kDa cortical protein. The 90‐kDa protein remained phosphorylated during cilia regeneration and then gradually became dephosphorylated. The 90‐kDa protein was phosphorylated and dephosphorylated normally in Tetrahymena mutants that assemble short cilia, suggesting that achievement of full length is not the signal that triggers dephosphorylation of the 90‐kDa protein. When initiation of cilia assembly is blocked, the 90‐kDa protein becomes phosphorylated and remains phosphorylated for an extended period of time, suggesting that initiation of cilia elongation triggers eventual dephosphorylation of the 90‐kDa protein, regardless of how long the cilia actually become.