Reading protein modifications with interaction domains
Top Cited Papers
- 1 July 2006
- journal article
- review article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 7 (7) , 473-483
- https://doi.org/10.1038/nrm1960
Abstract
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.Keywords
This publication has 73 references indexed in Scilit:
- Protein linguistics — a grammar for modular protein assembly?Nature Reviews Molecular Cell Biology, 2006
- Multisite protein modification and intramolecular signalingOncogene, 2004
- Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9Nature, 2002
- Modular phosphoinositide-binding domains – their role in signalling and membrane traffickingCurrent Biology, 2001
- The Sequence of the Human GenomeScience, 2001
- The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5pThe EMBO Journal, 2000
- The Molecular Basis of FHA Domain:Phosphopeptide Binding Specificity and Implications for Phospho-Dependent Signaling MechanismsMolecular Cell, 2000
- MODULAR PEPTIDE RECOGNITION DOMAINS IN EUKARYOTIC SIGNALINGAnnual Review of Biophysics, 1997
- Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptorNature, 1995
- Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free formsCell, 1993