Affinity-based assays for the identification and quantitative evaluation of noncovalent poly(ADP-ribose)-binding proteins

基于亲和力的检测方法用于鉴定和定量评估非共价聚(ADP-核糖)结合蛋白

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作者:Jean-Philippe Gagné, Jean-François Haince, Emilie Pic, Guy G Poirier

Abstract

Poly(ADP-ribose) polymerases have been linked to several cellular functions, most of which being mediated through the dynamics of poly(ADP-ribose) (pADPr). In several pathways, pADPr is the effector molecule that regulates cellular signaling and dictates biological outcomes. pAPDr is a central molecule that is capable of promoting both cell survival through the maintenance of genome integrity and cell death that occurs by way of a signal-mediated apoptotic-like process. Thus, interactions with pADPr are extremely important in bringing about the balanced regulation that controls cell fate. Further clues regarding these functions are emerging from a growing list of proteins with which pADPr interacts. Here, we describe the current approaches for investigating noncovalent protein interactions with pADPr.

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