Author Manuscript Published OnlineFirst on May 13, 2019; DOI: 10.1158/0008-5472.CAN-18-3658 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Disruption of the scaffolding function of mLST8 selectively inhibits mTORC2 assembly and function and suppresses mTORC2-dependent tumor growth in vivo Yoonha Hwang1,2*, Laura C. Kim3*, Wenqiang Song1,2, Deanna N. Edwards1,2, Rebecca S. Cook3,4,5,6, and Jin Chen1,2,3,5,6# 1Veterans Affairs Medical Center, Tennessee Valley Healthcare System, Nashville, Tennessee, USA. 2Division of Rheumatology and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee, USA. 3Program in Cancer Biology, Vanderbilt University, Nashville, Tennessee, USA. 4Deparment of Biomedical Engineering, Vanderbilt University, Nashville, Tennessee, USA. 5Vanderbilt-Ingram Cancer Center, Vanderbilt University Medical Center, Nashville, Tennessee, USA. 6Department of Cell and Developmental Biology, Vanderbilt University, Nashville, Tennessee, USA. *These two authors contributed equally. Running Title: Selective role of mLST8 in mTORC2 Keywords: mLST8, mTORC1, mTORC2, RICTOR, RAPTOR, SIN1 Conflicts of Interest: The authors declare that they have no competing interests. # Correspondence should be addressed to: Jin Chen, M.D., Ph.D. Professor of Medicine T-3207E, MCN Vanderbilt University Medical Center Nashville, TN 37232 Email:
[email protected]. Tel. 615-343-3819. Downloaded from cancerres.aacrjournals.org on September 29, 2021. © 2019 American Association for Cancer Research. Author Manuscript Published OnlineFirst on May 13, 2019; DOI: 10.1158/0008-5472.CAN-18-3658 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Abstract Mechanistic target of rapamycin (mTOR) is a serine/threonine kinase that acts in two distinct complexes, mTORC1 and mTORC2, and is dysregulated in many diseases including cancer.