Deciliation induces phosphorylation of a 90-kDa cortical protein in Tetrahymena thermophila

• Published in: The Journal of eukaryotic microbiology Vol. 42; no. 6; p. 742
• Main Authors: Gitz, D L, Pennock, D G
• Format: Journal Article
• Language: English
• Published: United States 01.11.1995
• Subjects: Animals; Antibodies - pharmacology; Blotting, Western; Cilia - physiology; Cytoskeleton - physiology; Cytoskeleton - ultrastructure; Electrophoresis, Polyacrylamide Gel; Molecular Weight; Mutation; Phosphoproteins - isolation & purification; Phosphoproteins - metabolism; Protozoan Proteins - isolation & purification; Protozoan Proteins - metabolism; Tetrahymena thermophila - physiology
• DOI: 10.1111/j.1550-7408.1995.tb01626.x
• ISSN: 1066-5234

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.