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PMID: 18619997 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

Intrinsic disorder in scaffold proteins: getting more from less.

Progress in biophysics and molecular biology ·Vol. 98 ·No. 1 ·2008-09-00 ·Pages 85-106

Cortese MS, Uversky VN, Dunker AK

Abstract

Regulation, recognition and cell signaling involve the coordinated actions of many players. Signaling scaffolds, with their ability to bring together proteins belonging to common and/or interlinked pathways, play crucial roles in orchestrating numerous events by coordinating specific interactions among signaling proteins. This review examines the roles of intrinsic disorder (ID) in signaling scaffold protein function. Several well-characterized scaffold proteins with structurally and functionally characterized ID regions are used here to illustrate the importance of ID for scaffolding function. These examples include scaffolds that are mostly disordered, only partially disordered or those in which the ID resides in a scaffold partner. Specific scaffolds discussed include RNase, voltage-activated potassium channels, axin, BRCA1, GSK-3beta, p53, Ste5, titin, Fus3, BRCA1, MAP2, D-AKAP2 and AKAP250. Among the mechanisms discussed are: molecular recognition features, fly-casting, ease of encounter complex formation, structural isolation of partners, modulation of interactions between bound partners, masking of intramolecular interaction sites, maximized interaction surface per residue, toleration of high evolutionary rates, binding site overlap, allosteric modification, palindromic binding, reduced constraints for alternative splicing, efficient regulation via posttranslational modification, efficient regulation via rapid degradation, protection of normally solvent-exposed sites, enhancing the plasticity of interaction and molecular crowding. We conclude that ID can enhance scaffold function by a diverse array of mechanisms. In other words, scaffold proteins utilize several ID-facilitated mechanisms to enhance function, and by doing so, get more functionality from less structure.

MeSH Terms
Allosteric Site Alternative Splicing Animals Binding Sites Biological Evolution Biophysics/methods Humans Models, Biological Molecular Conformation Protein Binding Protein Conformation Protein Folding Proteins/chemistry Signal Transduction Solvents/chemistry
Chemicals
Proteins Solvents
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cortese Marc S
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Uversky Vladimir N
Dunker A Keith
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Article Info
Journal
Progress in biophysics and molecular biology
Abbr.
Prog Biophys Mol Biol
ISSN
0079-6107
DOI
10.1016/j.pbiomolbio.2008.05.007
Published
2008-09-00
Epub
2008-00-20
Pages
85-106
Language
English
Region
England
NLM ID
0401233
PMCID
PMC2671330
Subset
IM
Grants
NIGMS NIH HHS · R01 GM071714 · United States
NIGMS NIH HHS · R01 GM071714-01A2 · United States
NLM NIH HHS · R01 LM007688 · United States
NLM NIH HHS · R01 LM007688-01A1 · United States
External Links
PubMed source DOI: 10.1016/j.pbiomolbio.2008.05.007 PMC Full Text View journal details
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