Juvenile hormone stimulated tyrosine kinase-mediated protein phosphorylation in the CNS of the silk worm, Bombyx mori.
In vitro studies with the larval CNS of the silkworm, Bombyx mori revealed the phosphorylation of a 48-kDa protein, which was not dependent on cyclic nucleotides. Studies also revealed modest phosphorylation of this protein by a calcium-dependent but calmodulin-independent mechanism. However, phosphorylation of this protein was greatly enhanced in the presence of juvenile hormone (JH) I by a calcium-independent mechanism. This stimulatory effect of JH was seen in both homogenates as well as in intact CNS of Bombyx. Immunoblotting studies revealed the cross-reaction of this 48-kDa protein with phosphotyrosine monoclonal antibody and the phosphorylation of this protein was inhibited by genistein. This study suggests that the 48-kDa protein is a substrate for tyrosine kinase. The phosphorylation of this protein was also observed in other larval tissues such as salivary gland, fat body, and epidermis of Bombyx.
Department of Animal Sciences, School of Life Sciences, University of Hyderabad, Hyderabad, India.
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Arif
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Shanavas
Ch R K
ChR
Murthy
Aparna
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Dutta-Gupta
D000818:Animals; D012831:Bombyx / Q000378:metabolism; D002490:Central Nervous System / Q000378:metabolism*; D019476:Insect Proteins / Q000378:metabolism*; D007605:Juvenile Hormones / Q000378:metabolism*; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D012717:Sesquiterpenes / Q000378:metabolism*
D019476:Insect Proteins; D007605:Juvenile Hormones; D012717:Sesquiterpenes; C008442:juvenile hormone I; D011505:Protein-Tyrosine Kinases