Regulation of Hsp70 in excitatory neurons: possible implications for neuronal functioning

Abstract

Neurons maintain an intricate organization of cytoplasmic and membrane proteins for their integrity, quick communication across synapses and for other complex activities. Molecular chaperones such as members of the 70 kDa heat shock protein (HSP70) family may play very important roles in these functions. However, in spite of a recent report suggesting the presence of HSP70 related proteins in the synaptic vesicle docking complex at presynaptic sites and the known significant roles for HSP70 in excitotoxicity, there are remarkably few studies that have explored the potential role of HSP70 family proteins in physiological functions of neurons. Here we bring together direct and indirect evidences which suggest that several different pathways involved in long-term potentiation can influence the HSP70 levels at the synapse and hypothesize on possible physiological significance of this family of proteins in neuronal functions.