Interactions via intrinsically disordered regions: What kind of motifs?

Rita Pancsa, M. Fuxreiter

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

Proteins containing intrinsically disordered (ID) regions are widespread in eukaryotic organisms and are mostly utilized in regulatory processes. ID regions can mediate binary interactions of proteins or promote organization of large assemblies. Post-translational modifications of ID regions often serve as decision points in signaling pathways. Why Nature distinguished ID proteins in molecular recognition functions? In a simple view, binding of ID regions is accompanied by a large entropic penalty as compared to folded proteins. Even in complexes however, ID regions can preserve their conformational freedom, thereby recruit further partners and perform various functions. What sort of benefits ID regions offer for molecular interactions and which properties are exploited in the corresponding complexes? Here, we review models explaining the recognition mechanisms of ID proteins. Motif-based interactions are central to all proposed scenarios, including prestructured elements, anchoring sites and linear motifs. We aim to extract consensus features of the models, which could be used to predict ID-binding sites for a variety of partners.

Original languageEnglish
Pages (from-to)513-520
Number of pages8
JournalIUBMB Life
Volume64
Issue number6
DOIs
Publication statusPublished - Jun 2012

Fingerprint

Intrinsically Disordered Proteins
Molecular recognition
Proteins
Molecular interactions
Post Translational Protein Processing
Binding Sites
Organizations

Keywords

  • fuzzy complex
  • intrinsically disordered protein
  • linear motif
  • molecular recognition
  • preformed element

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Clinical Biochemistry
  • Molecular Biology
  • Genetics

Cite this

Interactions via intrinsically disordered regions : What kind of motifs? / Pancsa, Rita; Fuxreiter, M.

In: IUBMB Life, Vol. 64, No. 6, 06.2012, p. 513-520.

Research output: Contribution to journalArticle

@article{733748b22d9742ffb6cf1277b06a3ab0,
title = "Interactions via intrinsically disordered regions: What kind of motifs?",
abstract = "Proteins containing intrinsically disordered (ID) regions are widespread in eukaryotic organisms and are mostly utilized in regulatory processes. ID regions can mediate binary interactions of proteins or promote organization of large assemblies. Post-translational modifications of ID regions often serve as decision points in signaling pathways. Why Nature distinguished ID proteins in molecular recognition functions? In a simple view, binding of ID regions is accompanied by a large entropic penalty as compared to folded proteins. Even in complexes however, ID regions can preserve their conformational freedom, thereby recruit further partners and perform various functions. What sort of benefits ID regions offer for molecular interactions and which properties are exploited in the corresponding complexes? Here, we review models explaining the recognition mechanisms of ID proteins. Motif-based interactions are central to all proposed scenarios, including prestructured elements, anchoring sites and linear motifs. We aim to extract consensus features of the models, which could be used to predict ID-binding sites for a variety of partners.",
keywords = "fuzzy complex, intrinsically disordered protein, linear motif, molecular recognition, preformed element",
author = "Rita Pancsa and M. Fuxreiter",
year = "2012",
month = "6",
doi = "10.1002/iub.1034",
language = "English",
volume = "64",
pages = "513--520",
journal = "IUBMB Life",
issn = "1521-6543",
publisher = "Wiley-Blackwell",
number = "6",

}

TY - JOUR

T1 - Interactions via intrinsically disordered regions

T2 - What kind of motifs?

AU - Pancsa, Rita

AU - Fuxreiter, M.

PY - 2012/6

Y1 - 2012/6

N2 - Proteins containing intrinsically disordered (ID) regions are widespread in eukaryotic organisms and are mostly utilized in regulatory processes. ID regions can mediate binary interactions of proteins or promote organization of large assemblies. Post-translational modifications of ID regions often serve as decision points in signaling pathways. Why Nature distinguished ID proteins in molecular recognition functions? In a simple view, binding of ID regions is accompanied by a large entropic penalty as compared to folded proteins. Even in complexes however, ID regions can preserve their conformational freedom, thereby recruit further partners and perform various functions. What sort of benefits ID regions offer for molecular interactions and which properties are exploited in the corresponding complexes? Here, we review models explaining the recognition mechanisms of ID proteins. Motif-based interactions are central to all proposed scenarios, including prestructured elements, anchoring sites and linear motifs. We aim to extract consensus features of the models, which could be used to predict ID-binding sites for a variety of partners.

AB - Proteins containing intrinsically disordered (ID) regions are widespread in eukaryotic organisms and are mostly utilized in regulatory processes. ID regions can mediate binary interactions of proteins or promote organization of large assemblies. Post-translational modifications of ID regions often serve as decision points in signaling pathways. Why Nature distinguished ID proteins in molecular recognition functions? In a simple view, binding of ID regions is accompanied by a large entropic penalty as compared to folded proteins. Even in complexes however, ID regions can preserve their conformational freedom, thereby recruit further partners and perform various functions. What sort of benefits ID regions offer for molecular interactions and which properties are exploited in the corresponding complexes? Here, we review models explaining the recognition mechanisms of ID proteins. Motif-based interactions are central to all proposed scenarios, including prestructured elements, anchoring sites and linear motifs. We aim to extract consensus features of the models, which could be used to predict ID-binding sites for a variety of partners.

KW - fuzzy complex

KW - intrinsically disordered protein

KW - linear motif

KW - molecular recognition

KW - preformed element

UR - http://www.scopus.com/inward/record.url?scp=84861327457&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84861327457&partnerID=8YFLogxK

U2 - 10.1002/iub.1034

DO - 10.1002/iub.1034

M3 - Article

C2 - 22535488

AN - SCOPUS:84861327457

VL - 64

SP - 513

EP - 520

JO - IUBMB Life

JF - IUBMB Life

SN - 1521-6543

IS - 6

ER -