Dephosphorylation of a 30-kDa protein of fowl spermatozoa by the addition of myosin light chain kinase substrate peptide inhibits the flagellar motility

Biochemical and Biophysical Research Communications
K AshizawaY Tsuzuki


Phosphorylation of demembranated fowl sperm proteins during incubation with [gamma-32P]ATP and various protein kinase substrate peptides at 30 degrees C was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). A marked difference in phosphorylation was observed in a 30 kDa protein. This protein was strongly phosphorylated after the addition of Kemptide, a cAMP-dependent protein kinase (PKA) substrate peptide; Syntide 2, a calmodulin-dependent protein kinase II substrate peptide; a protein kinase C (PKC) substrate peptide; as well as control samples but only slightly phosphorylated in the presence of a myosin light chain kinase (MLCK) substrate peptide. The motility of demembranated spermatozoa at 30 degrees C remained high in control samples and following the addition of Kemptide, Syntide 2 and PKC substrate peptide, but decreased markedly following the addition of MLCK substrate peptide. These results suggest that the 30 kDa protein is identified as a substrate for MLCK or a MLCK-like protein in fowl spermatozoa and that phosphorylation-dephosphorylation of this protein is involved in the regulation of flagellar movement at 30 degrees C.


Oct 31, 2003·Biology of Reproduction·Mohammad H ModarressiFrans A van der Hoorn
May 10, 2005·Biology of Reproduction·George G Ignotz, Susan S Suarez
Jan 28, 1998·Molecular Reproduction and Development·K AshizawaY Tsuzuki
Oct 30, 1998·Biochemical and Biophysical Research Communications·J S Tash, G E Bracho

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