Related Experiment Video
Updated: Jun 5, 2026
Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
From sequence to structural analysis in protein phosphorylation motifs
Allegra Via1, Francesca Diella, Toby James Gibson
1Biocomputing Group, Department of Biochemical Science A Rossi Fanelli, Sapienza University of Rome, P le Aldo Moro 5, Rome, Italy.
Abstract:
Phosphorylation is the most widely studied post-translational modification occurring in cells. While mass spectrometry-based proteomics experiments are uncovering thousands of novel in vivo phosphorylation sites, the identification of kinase specificity rules still remains a relatively slow and often inefficacious task. In the last twenty years, many efforts have being devoted to the experimental and computational identification of sequence and structural motifs encoding kinase-substrate interaction key residues and the phosphorylated amino acid itself. In this review, we retrace the road to the discovery of phosphorylation sequence motifs, examine the progresses achieved in the detection of three-dimensional motifs and discuss their importance in the understanding of regulation and de-regulation of many cellular processes.
Insights
Identifying kinase specificity rules is crucial for understanding cell regulation. This review explores sequence and structural motifs that govern phosphorylation, a key post-translational modification, to improve identification efficiency.
Area of Science:
- Molecular Biology
- Biochemistry
- Proteomics
Background:
- Phosphorylation is a critical post-translational modification regulating cellular processes.
- Identifying kinase specificity rules is challenging despite advances in proteomics.
- Understanding these rules is key to deciphering cellular regulation.
Purpose of the Study:
- To review the discovery of phosphorylation sequence motifs.
- To examine progress in detecting three-dimensional (3D) structural motifs.
- To discuss the importance of these motifs in cellular regulation.
Main Methods:
- Literature review of experimental and computational approaches.
- Analysis of identified sequence motifs.
- Examination of structural motif detection methods.
Main Results:
- Numerous sequence and structural motifs governing kinase-substrate interactions have been identified.
- Progress has been made in detecting 3D motifs, enhancing understanding of specificity.
- These motifs are vital for comprehending cellular process regulation.
Conclusions:
- Advances in identifying sequence and structural motifs are improving kinase specificity rule discovery.
- Understanding these motifs is essential for studying cellular regulation and disease.
- Further research into 3D motifs holds promise for future insights.
Related Concept Videos
02:54Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
02:54Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
01:02Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
01:02Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
01:30Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
01:56Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...