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.
Arif
A
A
Department of Animal Sciences, School of Life Sciences, University of Hyderabad, Hyderabad, India.
Shanavas
A
A
Murthy
Ch R K
ChR
Dutta-Gupta
Aparna
A
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