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Patricia Nagnan-Le Meillour Chrystelle Le Danvic Fanny Brimau Philippe Chemineau Jean-Claude Michalski 《Journal of chemical ecology》2009,35(7):752-760
The identification of various isoforms of olfactory binding proteins is of major importance to elucidate their involvement
in detection of pheromones and other odors. Here, we report the characterization of the phosphorylation of OBP (odorant binding
protein) and Von Ebner’s gland protein (VEG) from the pig, Sus scrofa. After labeling with specific antibodies raised against the three types of phosphorylation (Ser, Thr, Tyr), the phosphate-modified
residues were mapped by using the beta-elimination followed by Michael addition of dithiothreitol (BEMAD) method. Eleven phosphorylation
sites were localized in the pOBP sequence and nine sites in the VEG sequence. OBPs are secreted by Bowman’s gland cells in
the extracellular mucus lining the nasal cavity. After tracking the secretion pathway in the rough endoplasmic reticulum of
these cells, we hypothesize that these proteins may be phosphorylated by ectokinases that remain to be characterized. The
existence of such a regulatory mechanism theoretically increases the number of OBP variants, and it suggests a more specific
role for OBPs in odorant coding than the one of odorant solubilizer and transporter.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.
Chrystelle Le Danvic and Fanny Brimau contributed equally to the work. 相似文献