| Literature DB >> 31780625 |
Ina Yoon1, Miso Nam2, Hoi Kyoung Kim1, Hee-Sun Moon1, Sungmin Kim1, Jayun Jang3, Ji Ae Song3, Seung Jae Jeong1, Sang Bum Kim1, Seongmin Cho3, YounHa Kim3, Jihye Lee1, Won Suk Yang1, Hee Chan Yoo4, Kibum Kim4,5, Min-Sun Kim2, Aerin Yang6, Kyukwang Cho6, Hee-Sung Park6, Geum-Sook Hwang2, Kwang Yeon Hwang7, Jung Min Han4,5, Jong Hyun Kim8, Sunghoon Kim8,3.
Abstract
Despite the importance of glucose and amino acids for energy metabolism, interactions between the two nutrients are not well understood. We provide evidence for a role of leucyl-tRNA synthetase 1 (LARS1) in glucose-dependent control of leucine usage. Upon glucose starvation, LARS1 was phosphorylated by Unc-51 like autophagy activating kinase 1 (ULK1) at the residues crucial for leucine binding. The phosphorylated LARS1 showed decreased leucine binding, which may inhibit protein synthesis and help save energy. Leucine that is not used for anabolic processes may be available for catabolic pathway energy generation. The LARS1-mediated changes in leucine utilization might help support cell survival under glucose deprivation. Thus, depending on glucose availability, LARS1 may help regulate whether leucine is used for protein synthesis or energy production.Entities:
Mesh：
Substances：
Year: 2019 PMID： 31780625 DOI： 10.1126/science.aau2753
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728