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dc.contributor.author
Sluchanko, Nikolai N.  
dc.contributor.author
Bustos, Diego Martin  
dc.date.available
2020-12-28T15:48:22Z  
dc.date.issued
2019-01  
dc.identifier.citation
Sluchanko, Nikolai N.; Bustos, Diego Martin; Intrinsic disorder associated with 14-3-3 proteins and their partners; Elsevier; Progress In Molecular Biology And Translational Science; 166; 1-2019; 19-61  
dc.identifier.issn
1878-0814  
dc.identifier.uri
http://hdl.handle.net/11336/121220  
dc.description.abstract
Protein-protein interactions (PPIs) mediate a variety of cellular processes and form complex networks, where connectivity is achieved owing to the “hub” proteins whose interaction with multiple protein partners is facilitated by the intrinsically disordered protein regions (IDPRs) and posttranslational modifications (PTMs). Universal regulatory proteins of the eukaryotic 14-3-3 family nicely exemplify these concepts and are the focus of this chapter. The extremely wide interactome of 14-3-3 proteins is characterized by high levels of intrinsic disorder (ID) enabling protein phosphorylation and consequent specific binding to the well-structured 14-3-3 dimers, one of the first phosphoserine/phosphothreonine binding modules discovered. However, high ID enrichment also challenges structural studies, thereby limiting the progress in the development of small molecule modulators of the key 14-3-3 PPIs of increased medical importance. Besides the well-known structural flexibility of their variable C-terminal tails, recent studies revealed the strong and conserved ID propensity hidden in the N-terminal segment of 14-3-3 proteins (~ 40 residues), normally forming the α-helical dimerization region, that may have a potential role for the dimer/monomer dynamics and recently reported moonlighting chaperone-like activity of these proteins. We review the role of ID in the 14-3-3 structure, their interactome, and also in selected 14-3-3 complexes. In addition, we discuss approaches that, in the future, may help minimize the disproportion between the large amount of known 14-3-3 partners and the small number of 14-3-3 complexes characterized with atomic precision, to unleash the whole potential of 14-3-3 PPIs as drug targets.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
FOLDING UPON BINDING  
dc.subject
INTERACTOME  
dc.subject
MOLECULAR RECOGNITION  
dc.subject
PHOSPHORYLATION  
dc.subject
PROTEIN DOMAIN  
dc.subject
PROTEIN STRUCTURE  
dc.subject
PROTEIN-PROTEIN INTERACTION NETWORKS  
dc.subject
PROTEIN-PROTEIN INTERACTIONS  
dc.subject.classification
Biología Celular, Microbiología  
dc.subject.classification
Ciencias Biológicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
Intrinsic disorder associated with 14-3-3 proteins and their partners  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2020-11-19T22:02:47Z  
dc.journal.volume
166  
dc.journal.pagination
19-61  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Sluchanko, Nikolai N.. Moscow State University; Rusia. Russian Academy of Sciences; Rusia  
dc.description.fil
Fil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina  
dc.journal.title
Progress In Molecular Biology And Translational Science  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/bs.pmbts.2019.03.007  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1877117319300419