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The Journal of General Physiology, Vol 74, 565-582, Copyright © 1979 by The Rockefeller University Press
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PJ Stein, JD Brammer and SE Ostroy
Mosquito rhodopsin is a digitonin-soluble membrane protein of molecular weight 39,000 daltons, as determined by sodium dodecyl sulfate gel electrophoresis. The rhodopsin undergoes a spectral transition from R515-520 to M480 after orange illumination. The visual pigment apoprotein, opsin, is the major membrane protein in the eye. Protein synthesis in the photoreceptor cells occurs in the perinuclear cytoplasm and the newly made protein is transported to the rhabdom. Light adaptation increases the rate of turnover of this rhabdomal protein. The turnover of electrophoretically isolated opsin is also stimulated by light adaptation. The changes observed in protein metabolism biochemically, are consistent with previous morphological observations of photoreceptor membrane turnover. The results agree with the hypothesis that the newly synthesized rhabdomal protein is opsin.
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  U. Acharya, M. B. Mowen, K. Nagashima, and J. K. Acharya Ceramidase expression facilitates membrane turnover and endocytosis of rhodopsin in photoreceptors PNAS, February 17, 2004; 101(7): 1922 - 1926. [Abstract] [Full Text] [PDF]
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