XB-ART-29069
Mol Cell Endocrinol
1985 Sep 01;422:127-33. doi: 10.1016/0303-7207(85)90100-5.
Show Gene links
Show Anatomy links
Characterization of alpha-MSH-induced changes in the phosphorylation of a 53 kDa protein in Xenopus melanophores.
???displayArticle.abstract???
alpha-Melanotropin has been shown to induce specific changes in the degree of phosphorylation of a 53 kDa melanophore protein, concomitant with pigment dispersion. To further characterize the alpha-MSH-induced changes in 53 kDa phosphorylation in melanophores from the ventral tail-fin of Xenopus tadpoles, we investigated the concentration and time dependency of the effect. A significant increase in 53 kDa phosphorylation was detectable at 5 X 10(-8) M alpha-MSH. The maximal increase in 53 kDa phosphorylation was found after an incubation time of 10-15 min, whereas pigment dispersion was optimal after 60 min. The phosphorylated 53 kDa band showed clear cross-reactivity with monoclonal anti-beta-tubulin, and migrates as a single protein after two-dimensional (2D) separation. On a 2D-separation system the 53 kDa protein (IEP 5.1) migrated in the acidic tail of purified beta-tubulin. Our data strongly indicate that the 53 kDa protein is a beta-tubulin-like protein. We suggest that the degree of 53 kDa phosphorylation may be an important factor in the regulation of microtubule function in melanophores.
???displayArticle.pubmedLink??? 4065423
???displayArticle.link??? Mol Cell Endocrinol
Species referenced: Xenopus laevis
Genes referenced: pomc