Speaker：：Sheng-Cai Lin
School of Life Sciences, Xiamen University, China
Location: Conference Hall, Division of Biotechnology,
Dalian Institute of Chemical Physics，CAS
Time: 2016.3.18 (Friday) 10:00- 11:30 p.m.
CV of the speaker:
SHENG-CAI LIN, Ph.D., Professor, Dean
School of Life Sciences, Xiamen University
Fujian 361102, Xiamen, China
Telephone: (86)-592-2182993
Facsimile: (86)-592-2182993
E-mail: linsc@xmu.edu.cn
EDUCATION
1980-1984 B.S., Biology, Xiamen (Amoy) University
1984-1985 English Language, Zhongshan University
1985-1991 Ph.D., Biochemistry, University of Texas
Southwestern Medical Center at Dallas
EMPLOYMENT EXPERIENCE
1991-1995 Associate, Howard Hughes Medical Institute, University of California, San Diego
1995- 2001 Senior Scientist (Assistant Professor), Institute of Molecular and Cell Biology (IMCB), National University of Singapore
2001-2004. Assistant Professor, Department of Biochemistry, Hong Kong University of Science& Technology
July, 2004-06 Associate Professor (with tenure), Department of Biochemistry, Hong Kong University of Science& Technology
July, 2001-present: Professor, School of Life Sciences, Xiamen University
2001-Present: Cheung Kong Scholar, School of Life Sciences,
Xiamen University;
2003-present: Dean, School of Life Sciences, Xiamen University
Abstract：Metabolic homeostasis is maintained by various cellular sensors, including the master kinases AMPK (AMP-activated protein kinase) and mTORC1. In response to low energy status, AMPK is activated to enhance catabolic activities with concurrent inhibition of anabolic processes such as fatty acid synthesis. In contrast, mTORC1 is activated when nutrients and growth factors are abundant. Previously, we discovered the mechanism by which AMP, as a low energy-charge signal, can autonomously initiate the assembly of an activating complex for AMPK in response to starvation. AMP binding causes a higher affinity of AMPK for the scaffold protein AXIN that also binds to LKB1, thereby promoting phosphorylation and activation of AMPK. More recently, we found most surprisingly that the late endosomal/lysosomal protein complex v-ATPase-Ragulator, essential for activation of mTORC1, is also required for AMPK activation. We also uncovered that AMPK is a residential protein of late endosome/lysosome. Under glucose starvation, the v-ATPase-Ragulator complex is accessible to AXIN/LKB1 for AMPK activation. Concurrently, mTORC dissociates from endosome and becomes inactivated. We have thus revealed a switch between catabolism and anabolism.
Most recently, we have uncovered other functions of ULK1/2 kinases than initiation of autophagy. We found that ULK1 functions to regulate glycolytic pathways by direct phosphorylation of multiple glycolytic enzymes. The functional outcome of the modulation of the enzymatic activities by ULK1 will be presented at the talk.
Contact:：Group 18M0, Prof. Hai-long Piao（82463004）