Multiple binding partners
1Department of Biochemistry, Kansas City University of Medicine and Biosciences, Kansas City, MO, USA.
Abstract:
GAPDH interacts with a plethora of diverse cellular proteins. The network of interacting partners, or interactome, is presented for GAPDH with the interacting molecules grouped into specific functional and structural categories. By organizing the binding partners in this way, certain common structural features are beginning to surface, such as acidic dipeptide sequences that are found in several of these binding proteins. Additionally, the consensus sequences for target polynucleotides are being brought to light. The categories, which are presented according to function, offer an opportunity for research into the corresponding structural correlates to these interactions. Recent discoveries of interacting proteins have revealed novel relationships that are generating emerging mechanisms. Proteins that are associated with age-related neurodegenerative diseases appear to be particularly prone to binding GAPDH, suggesting that GAPDH may be playing a role in these diseases. Neurodegenerative diseases that are discussed are the conformational diseases of aging, suggesting that GAPDH may be a global sensor for cellular conformational stress. In addition to GAPDH's oxidoreductase activity, several other enzymatic functions have been discovered, including peroxidase, nitrosylase, mono-ADP-ribosylase and kinase activities.
More Related Videos
10:17Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
Published on: January 14, 2020
06:45Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
Published on: June 15, 2018
Related Concept Videos
Ligand Binding and Linkage
Ligand Binding and Linkage
Cooperative Binding of Transcription Regulators
Cooperative Binding of Transcription Regulators
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
