Phosphorylation of native porcine olfactory binding proteins
Patricia Nagnan-Le Meillour1, Chrystelle Le Danvic, Fanny Brimau
1INRA, UMR 8576 CNRS/Université Lille1, Unité de Glycobiologie Structurale et Fonctionnelle, F-59655, Villeneuve d'Ascq, Cedex, France. patricia.le-meillour@univ-lille1.fr
Journal of Chemical Ecology
|July 7, 2009
Summary
Researchers characterized phosphorylation in pig odorant binding proteins (OBPs) and Von Ebner's gland proteins (VEGs). This finding suggests a more specific role for OBPs in odorant coding beyond simple transport.
Area of Science:
- Olfactory receptor research
- Protein biochemistry
- Mammalian physiology
Background:
- Olfactory binding proteins (OBPs) and Von Ebner's gland proteins (VEGs) are crucial for detecting odors and pheromones.
- Understanding protein modifications like phosphorylation is key to elucidating their function.
Purpose of the Study:
- To characterize the phosphorylation of OBP and VEG in pigs (Sus scrofa).
- To identify specific phosphorylation sites on these proteins.
Main Methods:
- Antibody labeling for Ser, Thr, and Tyr phosphorylation.
- Beta-elimination followed by Michael addition of dithiothreitol (BEMAD) for residue mapping.
Main Results:
- Eleven phosphorylation sites were identified in the pOBP sequence.
- Nine phosphorylation sites were identified in the VEG sequence.
Conclusions:
- Phosphorylation of OBPs and VEGs suggests a regulatory mechanism.
- This modification may indicate a more specific role for OBPs in odorant coding than previously thought.
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