Wagner V, Kreimer G, Mittag M (2008)
Publication Status: Published
Publication Type: Journal article, Short survey
Publication year: 2008
Publisher: Landes Bioscience
Book Volume: 3
Pages Range: 433-435
Journal Issue: 7
DOI: 10.4161/psb.3.7.5685
One of the key modifications of proteins that can affect protein functions, activities, stabilities, localizations and interactions, represents phosphorylation. For functional phosphoproteomics, phosphopeptides are enriched from isolated sub-cellular fractions of interest and analyzed by liquid chromatography-electrospray ionization-mass spectrometry. Such an approach was recendy applied to the eyespot apparatus of the green flagellate alga Chlamydomonas reinhardtii, which represents a primordial visual system. Thereby, 32 phosphoproteins of known eyespot proteins along with 52 precise in vivo phosphorylation sites were identified. They include enzymes of carotenoid and fatty acid metabolism, (putative) light signaling components and proteins with unknown function. Strikingly, the two unique green algal photoreceptors, channelrhodopsin-1 and -2 were found to be phosphorylated in the cytoplasmic loop next to their seven transmembrane regions in a similar distance as observed in vertebrate rhodopsins. ©2008 Landes Bioscience.
APA:
Wagner, V., Kreimer, G., & Mittag, M. (2008). The power of functional proteomics: Components of the green algal eyespot and its light signaling pathway(s). Plant Signaling & Behavior, 3(7), 433-435. https://doi.org/10.4161/psb.3.7.5685
MLA:
Wagner, Volker, Georg Kreimer, and Maria Mittag. "The power of functional proteomics: Components of the green algal eyespot and its light signaling pathway(s)." Plant Signaling & Behavior 3.7 (2008): 433-435.
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