Deciliation induces phosphorylation of a 90-kDa cortical protein in Tetrahymena thermophila.
We have used the anti-phosphoprotein antibody MPM-2 to examine changes in phosphorylation 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.
Department of Zoology, Miami University, Oxford, Ohio 45056, USA.
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D000818:Animals; D000906:Antibodies / Q000494:pharmacology; D015153:Blotting, Western; D002923:Cilia / Q000502:physiology*; D003599:Cytoskeleton / Q000502:physiology / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009154:Mutation; D010750:Phosphoproteins / Q000302:isolation & purification / Q000378:metabolism*; D015800:Protozoan Proteins / Q000302:isolation & purification / Q000378:metabolism*; D016808:Tetrahymena thermophila / Q000502:physiology*
D000906:Antibodies; D010750:Phosphoproteins; D015800:Protozoan Proteins