The role of anchoring protein RACK1 in PKC activation in the ageing rat brain

High levels of expression of Ca2+/phospholipid-dependent protein kinase C (PKC) occur in neuronal tissues and play a strategic role in the modulation of short-and long-term functions (ion channels, receptor desensitization, neurotransmitter release and synaptic efficiency) that become modified during the brain ageing process. Recent studies have clarified the key role played by the anchoring proteins in mediating subcellular PKC location, that is, in driving the enzyme to specific sites of action. The protein, receptor far activated C-kinase I (RACK I) is involved in PKC-mediated signal transduction. A postnatal developmental increase in RACK I levels indicates their significance in the outgrowth of neuronal processes. In a physiological model of impairment in PKC translocation - the aged rat brain cortex - RACK I levels are reduced and the PKC isoenzymes known to interact with it do not translocate to membrane compartments upon stimulation. Anchoring proteins might represent new targets for compounds that modulate PKC signal transduction processes.