INVESTIGADORES
BUSTOS Diego Martin
artículos
Título:
Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins
Autor/es:
UHART, MARINA; BUSTOS, DIEGO M
Revista:
Frontiers in Genetics
Editorial:
HFSP
Referencias:
Año: 2014 vol. 5 p. 10 - 15
Resumen:
The understanding of networks is a common goal of an unprecedented array
of traditional disciplines. One of the protein network properties most
influenced by the structural contents of its nodes is the
inter-connectivity. Recent studies in which structural information was
included into the topological analysis of protein networks revealed that
the content of intrinsic disorder in the nodes could modulate the
network topology, rewire networks, and change their inter-connectivity,
which is defined by its clustering coefficient. Here, we review the role
of intrinsic disorder present in the partners of the highly conserved
14-3-3 protein family on its interaction networks. The 14-3-3s are
phospho-serine/threonine binding proteins that have strong influence in
the regulation of metabolism and signal transduction networks. Intrinsic
disorder increases the clustering coefficients, namely the
inter-connectivity of the nodes within each 14-3-3 paralog networks. We
also review two new ideas to measure intrinsic disorder independently of
the primary sequence of proteins, a thermodynamic model and a method
that uses protein structures and their solvent environment. This new
methods could be useful to explain unsolved questions about versatility
and fixation of intrinsic disorder through evolution. The relation
between the intrinsic disorder and network topologies could be an
interesting model to investigate new implicitness of the graph theory
into biology.