Cited by 847Protein Structure and DynamicsReceptor Mechanisms and SignalingHeat shock proteins research

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Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

Uversky, Vladimir N., Oldfield, Christopher J., Dunker, A. Keith·2005·Journal of Molecular Recognition

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Abstract

Regulation, recognition and cell signaling involve the coordinated actions of many players. To achieve this coordination, each participant must have a valid identification (ID) that is easily recognized by the others. For proteins, these IDs are often within intrinsically disordered (also ID) regions. The functions of a set of well-characterized ID regions from a diversity of proteins are presented herein to support this view. These examples include both more recently described signaling proteins, such as p53, alpha-synuclein, HMGA, the Rieske protein, estrogen receptor alpha, chaperones, GCN4, Arf, Hdm2, FlgM, measles virus nucleoprotein, RNase E, glycogen synthase kinase 3beta, p21(Waf1/Cip1/Sdi1), caldesmon, calmodulin, BRCA1 and several other intriguing proteins, as well as historical prototypes for signaling, regulation, control and molecular recognition, such as the lac repressor, the voltage gated potassium channel, RNA polymerase and the S15 peptide associating with the RNA polymerase S-protein. The frequent occurrence and the common use of ID regions in important protein functions raise the possibility that the relationship between amino acid sequence, disordered ensemble and function might be the dominant paradigm for the molecular recognition that serves as the basis for signaling and regulation by protein molecules.

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Authors: Uversky, V. N., Oldfield, C. J., & Dunker, A. K.
Affiliations: Russian Academy of Sciences (RU)
Molecular Kinetics (United States) (US)
Corresponding author: Uversky, Vladimir N.
ORCID: Uversky, Vladimir N.
Oldfield, Christopher J.
Dunker, A. Keith
Venue: Journal of Molecular Recognition
Publisher: Wiley
Published: 2005
Volume: 18
Issue: 5
Pages: 343-384
ISSN: 0952-3499 (ISSN-L)
1099-1352
DOI: 10.1002/jmr.747
OpenAlex: W2162720882
Cited by: 847
References: 439
Citations by year: 2026: 15 · 2025: 14 · 2024: 23 · 2023: 28 · 2022: 31 · 2021: 27 · 2020: 37 · 2019: 48 · 2018: 33 · 2017: 46 · 2016: 38 · 2015: 47 · 2014: 53 · 2013: 55 · 2012: 56
FWCI: 3.87
Type: journal article
Language: en
Open access: closed
Licence: doi.wiley.com/10.1002/tdm_license_1.1 (tdm, 3895 d)
Locations: Journal of Molecular Recognition (publishedVersion)
PubMed (publishedVersion)
Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
Funders: U.S. National Library of Medicine (R01LM007688, 1 R01 LM007688-0A1)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: intrinsically disordered regions, protein recognition, signal transduction, protein regulation, molecular recognition, p53, alpha-synuclein, HMGA, estrogen receptor alpha, molecular chaperones, GCN4, ARF, MDM2, measles virus nucleoprotein, RNase E, glycogen synthase kinase-3β, p21, caldesmon, calmodulin, BRCA1, lac repressor, voltage-gated potassium channels, RNA polymerase, S protein, sequence-function relationships
MeSH terms: Animals, Antigens, Humans, Nucleic Acids, Protein Conformation, Proteins, Signal Transduction, Protein Folding, Molecular Chaperones

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Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

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