  During the last decade, network approaches became a powerful tool to describe
protein structure and dynamics. Here, we describe first the protein structure
networks of molecular chaperones, then characterize chaperone containing
sub-networks of interactomes called as chaperone-networks or chaperomes. We
review the role of molecular chaperones in short-term adaptation of cellular
networks in response to stress, and in long-term adaptation discussing their
putative functions in the regulation of evolvability. We provide a general
overview of possible network mechanisms of adaptation, learning and memory
formation. We propose that changes of network rigidity play a key role in
learning and memory formation processes. Flexible network topology provides
"learning competent" state. Here, networks may have much less modular
boundaries than locally rigid, highly modular networks, where the learnt
information has already been consolidated in a memory formation process. Since
modular boundaries are efficient filters of information, in the "learning
competent" state information filtering may be much smaller, than after memory
formation. This mechanism restricts high information transfer to the "learning
competent" state. After memory formation, modular boundary-induced segregation
and information filtering protect the stored information. The flexible networks
of young organisms are generally in a "learning competent" state. On the
contrary, locally rigid networks of old organisms have lost their "learning
competent" state, but store and protect their learnt information efficiently.
We anticipate that the above mechanism may operate at the level of both
protein-protein interaction and neuronal networks.
