Studying of Telomeric Protein–Protein Interactions by Bi-Molecular Fluorescence Complementation (BiFC) and Peptide Array-Based Assays
Wenbin Ma, Hyeung Kim, Zhou Songyang
Abstract
Wenbin Ma, Hyeung Kim, Zhou Songyang
Abstract
Studying protein-protein interactions is critical to our understanding of the signaling pathways. The Telomere Interactome is assembled around the telomeres and consists of proteins and factors from diverse pathways. Dissecting how this protein network contributes to telomere protection and length regulation requires the elucidation of the complex and dynamic interactions between the proteins within the interactome. Here, we focus on the Bi-molecular fluorescence complementation (BiFC) and peptide array methods that have proven vital in our studies of telomere protein interaction networks.
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Studying protein-protein interactions is critical to our understanding of the signaling pathways. The Telomere Interactome is assembled around the telomeres and consists of proteins and factors from diverse pathways. Dissecting how this protein network contributes to telomere protection and length regulation requires the elucidation of the complex and dynamic interactions between the proteins within the interactome. Here, we focus on the Bi-molecular fluorescence complementation (BiFC) and peptide array methods that have proven vital in our studies of telomere protein interaction networks.
Key concepts: Bimolecular fluorescence complementation, Interactome, Telomere, Protein–protein interaction, Biology, Computational biology, 14-3-3 protein, Cell biology