Identifying Glyceraldehyde 3-Phosphate Dehydrogenase as a Cyclic Adenosine Diphosphoribose Binding Protein by Photoaffinity Protein-Ligand Labeling Approach

Zhang, Kehui1,2; Sun, Wei2,3,4; Huang, Lihong2; Zhu, Kaiyuan2; Pei, Fen1; Zhu, Longchao2; Wang, Qian2; Lu, Yingying2; Zhang, Hongmin3,4; Jin, Hongwei1; Zhang, Li-He1; Zhang, Liangren1; Yue, Jianbo2

2017-01-11

10.1021/jacs.6b08088

Journal of the American Chemical Society   影响因子和分区

0002-7863

1520-5126

Cyclic adenosine diphosphoribose (cADPR), an endogenous nucleotide derived from nicotinamide adenine dinucleotide (NAD(+)), mobilizes Ca2+ release from endoplasmic reticulum (ER) via ryanodine receptors (RyRs), yet the bridging protein(s) between cADPR and RyRs remain(s) unknown. Here we synthesized a novel photoaffinity labeling (PAL) cADPR agonist, PAL-cIDPRE, and subsequently applied it to purify its binding proteins in human Jurkat T cells. We identified glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as one of the cADPR binding protein(s), characterized the binding affinity between cADPR and GAPDH in vitro by surface plasmon resonance (SPR) assay, and mapped cADPR's binding sites in GAPDH. We further demonstrated that cADPR induces the transient interaction between GAPDH and RyRs in vivo and that GAPDH knockdown abolished cADPR-induced Ca2+ release. However, GAPDH did not catalyze cADPR into any other known or novel compound(s). In summary, our data clearly indicate that GAPDH is the long-sought-after cADPR binding protein and is required for cADPR-mediated Ca2+ mobilization from ER via RyRs.

SCI ; EI ; IC

英语

NI论文

其他

[ITS/261/14]

Chemistry

Chemistry, Multidisciplinary

WOS:000392036900032

AMER CHEMICAL SOC

20172003667811

Binding energy ; Binding sites ; Cell membranes ; Nucleotides ; Proteins ; Surface plasmon resonance

Biological Materials and Tissue Engineering:461.2 ; Biology:461.9 ; Biochemistry:801.2 ; Physical Chemistry:801.4 ; Organic Compounds:804.1

Web of Science

1.Peking Univ, Sch Pharmaceut Sci, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China
2.City Univ Hong Kong, Dept Biomed Sci, Hong Kong, Hong Kong, Peoples R China
3.South Univ Sci & Technol China, Dept Biol, Shenzhen 518052, Peoples R China
4.South Univ Sci & Technol China, Shenzhen Key Lab Cell Microenvironm, Shenzhen 518052, Peoples R China

Zhang, Kehui,Sun, Wei,Huang, Lihong,et al. Identifying Glyceraldehyde 3-Phosphate Dehydrogenase as a Cyclic Adenosine Diphosphoribose Binding Protein by Photoaffinity Protein-Ligand Labeling Approach[J]. Journal of the American Chemical Society,2017,139(1):156-170.

Zhang, Kehui.,Sun, Wei.,Huang, Lihong.,Zhu, Kaiyuan.,Pei, Fen.,...&Yue, Jianbo.(2017).Identifying Glyceraldehyde 3-Phosphate Dehydrogenase as a Cyclic Adenosine Diphosphoribose Binding Protein by Photoaffinity Protein-Ligand Labeling Approach.Journal of the American Chemical Society,139(1),156-170.

Zhang, Kehui,et al."Identifying Glyceraldehyde 3-Phosphate Dehydrogenase as a Cyclic Adenosine Diphosphoribose Binding Protein by Photoaffinity Protein-Ligand Labeling Approach".Journal of the American Chemical Society 139.1(2017):156-170.