Abstract
Publisher Summary This chapter reviews the current knowledge on neuron-specific phosphoprotein, B-50, with special emphasis on its localization and possible function(s). The chapter discusses the evidence that leads to the formulation of the hypothesis that the degree of phosphorylation of B-50 may modulate receptor-mediated hydrolysis of polyphosphoinositides. It also summarizes old and new data suggesting that such a modulatory mechanism may underlie adrenocorticotropic hormone (ACTH)-induced excessive grooming and may be of relevance not only to some behavioral actions of melanocortins, but also to neurotrophic actions. In the rat brain synaptic plasma membranes (SPM), a great number of phosphoproteins can be identified. In recent years, several of these proteins have been characterized and for some proteins, a functional role in neurotransmission and membrane function has been documented. B-50 is an acidic, 48-kDa protein that is intimately associated with the synaptic membrane because it can only be solubilized in the presence of detergent. The purified protein displays microheterogeneity upon isoelectric focussing in a narrow pH gradient. Upon two-dimensional polyacrylamide gel electrophoresis, it can be resolved into four distinct protein spots (48kDa) that are in part interconvertible by exhaustive phosphorylation or dephosphorylation.
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