Proteome-wide microarray-based screening of PAR-binding proteins

Author:

Kang Bong Gu,Kang Sung-Ung,Kim Jae Jin,Kwon Ji-Sun,Gagné Jean-Philippe,Lee Seo Yun,Kim Soyeon,Sangwon Karl L.,Ha Shinwon,Jeong Jun Seop,Lee Yun-Il,Zhu Heng,Kim Dongsan,Poirier Guy G.,Kang Ho Chul,Dawson Valina L.,Dawson Ted M.ORCID

Abstract

SUMMARYPoly(ADP-ribose) (PAR) plays a crucial role in intracellular signaling and scaffolding through covalent modification or non-covalent binding to target proteins. The non- covalent binding PARylome has not been extensively characterized. Here we performed a PAR-binding screen using a human protein microarray that covers most of the human proteome to characterize the non-covalent binding PARylome. A total of 356 PAR- binding proteins were identified. The PAR-binding PARylome suggests that PAR- binding regulates a variety of biological processes beyond well-characterized DNA damage signaling and DNA repair. Proteins that may be reprogrammed by PAR-binding include signaling molecules, transcription factors, nucleic acid binding proteins, calcium binding proteins, ligases, oxidoreductases, enzymes, transferases, hydrolases, and receptors. The global database of PAR-binding proteins that we established will be a valuable tool for further in-depth analysis of the role of PARylation in a wide range of biological contexts.

Publisher

Cold Spring Harbor Laboratory

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