Allosteric mechanisms in receptor heteromers markedly increase the repertoire of receptor recognition and signaling. Of high importance is the altered function in the receptor heteromer versus the receptor homomer. Such a change in receptor function is mainly brought about by agonist induced allosteric receptor-receptor interactions and leads to functional and structural plasticity. Receptor-receptor interactions integrating synaptic and volume transmission signals participate in a significant way in modulating bidirectional synaptic plasticity and thus Hebbian plasticity. One molecular mechanism that can contribute to a change of synaptic weight may be represented by multiple interactions between plasma membrane receptors forming higher order heteroreceptor complexes via oligomerization at the pre- and post-junctional level. Such long-lived heteroreceptor complexes may play a significant role in learning and memory.
Keywords: G protein-coupled receptor; allosteric receptor–receptor interaction; learning; long term depression; long term potentiation; memory plasticity; receptor heteromer; receptor tyrosine kinase; striatum.