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Home> Events> Identification of Novel Post-translational Modifications to Decode Tumorigenesis and Metabolic Diseases
Identification of Novel Post-translational Modifications to Decode Tumorigenesis and Metabolic Diseases
Publish Date:2014/05/09   |   Click:5913

美国华人质谱学会会员赵英明教授及其领导的团队最近发表了两篇很有意义的关于蛋白修饰的学术论文。请看我们CASMSSecretary顾泽宗教授和Member Connections Committee为大家带来的报道。

 

Dr. Yingming Zhao at the 2013 CASMS Annual Meeting in Minneapolis (photo by Gu).

 

Protein function is controlled by many factors and can be dictated by the distinct array of modifications that occur after proteins are synthesized. Modifications that are unique to specific diseases, such as tumors or metabolic diseases, can inform about the origin of the disease (tumorigenesis) and provide a platform for designing treatment strategies.

With the recent publication of two high-impact research papers, biochemist and cancer biologist Dr. Yingming Zhao, an active member of CASMS and professor at the University of Chicago, is charting new territory in the understanding of protein post-translational modifications (or PTMs) by describing novel 'marks' on histones and metabolic enzymes.

Zhao and his collaborators recently reported in Nature Chemical Biology the identification of a new histone modification on lysine residues called lysine 2-hydroxyisobutyrylation (Khib). Using mass spectrometry and validation with chemical and biochemical methodology, this histone mark was identified at 67 lysine sites, including several not known to be modified in other ways.In another collaborative study published in the most recent issue of Cell Metabolism, Dr. Zhao and his group describe a new protein post-translational modification called lysine glutarylation (Kglu). They further characterized an enzyme called sirtuin 5 as being responsible for removing this modification from specific target proteins.

Importantly, their work sheds new light into the mechanisms responsible for a genetic disease caused by mutations in glutaryl CoA dehydrogenase called glutaric acidemia type I. These findings also broaden our understanding of sirtuin 5 and lay the foundation for future work by Dr. Zhao's group and others in defining the function of Kglu modifications in diseases such as metabolic diseases.

Dai, L., Peng, C., Montellier, E., Lu, Z., Chen, Y., Tan, M., Ishii, H., Debernardi, A., Buchou, T., Rousseausm, S., Jin, F., Deng, Z., Ren, B., Khochbin, S., Zhao, Y. Lysine 2-hydroxyisobutyrylation is a novel type of active histone marks. Nature Chemical Biology, 2014. 19: 605-617.

Tan, M., Peng, C., Anderson, K.A.,Chhoy, P., Xie, Z., Dai, L., Park, J.S., Chen, Y., Huang, H., Zhang, Y., Ro, J., Wagner, G.R., Green, M.F., Madsen, A.F., Schmiesing, J., Peterson, B.S., Xu, G., Ilkayeva, O.R., Muehlbauer, M.J., Braulke, T., Mühlhausen, C., Backos, D.S., Olsen, C.A., McGuire, P.J., Pletcher, S.D., Lombard, D.B., Hirschey, M.D., Zhao, Y. Lysine Glutarylation Is a Novel Protein Modification Regulated by SIRT5. Cell Metabolism, 2014. 10: 365-370.

CASMSMember Connections Committee会不定期的为大家带来和美华质谱学会相关的科研成果的报道。如果您有好的意见和建议,请在我们CASMSLinkedIn group和我们联系。

(reported on May 09, 2014)

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