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Biochemical and biophysical research communications v.494 no.3/4, 2017년, pp.581 - 586   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Characterization of the zinc-induced Shank3 interactome of mouse synaptosome

Lee, Yeunkum (Department of Neuroscience, College of Medicine, Korea University, Seoul, South Korea ); Ryu, Jae Ryun (Department of Biomedical Sciences, College of Medicine, Korea University, Seoul, South Korea ); Kang, Hyojin (HPC-enabled Convergence Technology Research Division, Korea Institute of Science and Technology Information, Daejeon, South Korea ); Kim, Yoonhee (Department of Neuroscience, College of Medicine, Korea University, Seoul, South Korea ); Kim, Shinhyun (Department of Neuroscience, College of Medicine, Korea University, Seoul, South Korea ); Zhang, Yinhua (Department of Neuroscience, College of Medicine, Korea University, Seoul, South Korea ); Jin, Chunmei (Department of Neuroscience, College of Medicine, Korea University, Seoul, South Korea ); Cho, Hyo Min (Department of Biomedical Sciences, College of Medicine, Korea University, Seoul, South Korea ); Kim, Won-Ki (Department of Neuroscience, College of Medicine, Korea University, Seoul, South Korea ); Sun, Woong (Department of Biomedical Sciences, College of Medicine, Korea University, Seoul, South Korea ); Han, Kihoon (Department of Neuroscience, College of Medicine, Korea );
  • 초록  

    Abstract Variants of the SHANK3 gene, which encodes a core scaffold protein of the postsynaptic density of excitatory synapses, have been causally associated with numerous brain disorders. Shank3 proteins directly bind zinc ions through their C-terminal sterile α motif domain, which enhances the multimerization and synaptic localization of Shank3, to regulate excitatory synaptic strength. However, no studies have explored whether zinc affects the protein interactions of Shank3, which might contribute to the synaptic changes observed after zinc application. To examine this, we first purified Shank3 protein complexes from mouse brain synaptosomal lysates that were incubated with different concentrations of ZnCl 2 , and analyzed them with mass spectrometry. We used strict criteria to identify 71 proteins that specifically interacted with Shank3 when extra ZnCl 2 was added to the lysate. To characterize the zinc-induced Shank3 interactome, we performed various bioinformatic analyses that revealed significant associations of the interactome with subcellular compartments, including mitochondria, and brain disorders, such as bipolar disorder and schizophrenia. Together, our results showing that zinc affected the Shank3 protein interactions of in vitro mouse synaptosomes provided an additional link between zinc and core synaptic proteins that have been implicated in multiple brain disorders. Highlights The synaptosomal Shank3 complexes incubated with different ZnCl 2 concentrations were analyzed by mass spectrometry. The 71 proteins that specifically interacted with Shank3 under extra ZnCl 2 conditions were identified. The zinc-induced Shank3 interactome is associated with mitochondria and brain disorders.


  • 주제어

    Shank3 .   Zinc .   Interactome .   Synaptosome .   Mass spectrometry.  

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