Reading protein modifications with interaction domains

Proteins are controlled by a vast and dynamic array of post-translational modifications, many of which create binding sites for specific protein-interaction domains. We propose that these domains, working together, read the state of the proteome and therefore couple post-translational modifications...

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Published inNature reviews. Molecular cell biology Vol. 7; no. 7; pp. 473 - 483
Main Authors Pawson, Tony, Seet, Bruce T, Dikic, Ivan, Zhou, Ming-Ming
Format Journal Article
LanguageEnglish
Published England Nature Publishing Group 01.07.2006
Subjects
Amino Acid Motifs
Cell Physiological Phenomena
Kinases
Lipids
Models, Molecular
Molecular Structure
Phosphorylation
Polypeptides
Protein Binding
Protein Conformation
Protein Processing, Post-Translational
Proteins
Proteins - chemistry
Proteins - genetics
Proteins - metabolism
New York
Canada
Toronto Ontario Canada
United States > US
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Summary:Proteins are controlled by a vast and dynamic array of post-translational modifications, many of which create binding sites for specific protein-interaction domains. We propose that these domains, working together, read the state of the proteome and therefore couple post-translational modifications to cellular organization. We also identify common strategies through which modification-dependent interactions synergize to regulate cell behaviour.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:1471-0072
1471-0080
DOI:10.1038/nrm1960