title: EMC6/TMEM93 suppresses glioblastoma proliferation by modulating autophagy.
abstract: EMC6 (endoplasmic reticulum membrane protein complex subunit 6), also known as transmembrane protein 93, is a novel positive autophagy regulator. In this report, we evaluated the anti-tumor activity of EMC6 in glioblastoma cells in vitro and in vivo. Our data show that overexpression of EMC6 in three glioblastoma cell lines (SHG44, U87 and U251) suppresses tumor cell growth by activating autophagy, but fails to induce cell apoptosis. EMC6-mediated autophagy was associated with inactivation of the PIK3CA/AKT/mTOR signaling pathway. Accordingly, EMC6 knockdown in glioblastoma cells had the opposite effect; it promoted cell growth. Overexpression of EMC6 also sensitized glioblastoma cells to the chemotherapy drug, temozolomide, to further suppress tumor growth. Our data indicate that EMC6-induced autophagy may play a positive role in suppressing the development of glioblastoma.
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
authors.forename: X
authors.initials: X
authors.lastname: Shen
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
authors.forename: S
authors.initials: S
authors.lastname: Kan
authors.affiliation: Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Science Center, Beijing, China.|Peking University Center for Human Disease Genomics, Peking University, Beijing, China.
authors.forename: J
authors.initials: J
authors.lastname: Hu
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
authors.forename: M
authors.initials: M
authors.lastname: Li
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.|Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
authors.forename: G
authors.initials: G
authors.lastname: Lu
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
authors.forename: M
authors.initials: M
authors.lastname: Zhang
authors.affiliation: Department of Cardiology, Peking University Third Hospital, Beijing, China.
authors.forename: S
authors.initials: S
authors.lastname: Zhang
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
authors.forename: Y
authors.initials: Y
authors.lastname: Hou
authors.affiliation: Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Science Center, Beijing, China.|Peking University Center for Human Disease Genomics, Peking University, Beijing, China.
authors.forename: Y
authors.initials: Y
authors.lastname: Chen
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
authors.forename: Y
authors.initials: Y
authors.lastname: Bai
mesh_terms: D000818:Animals; D001343:Autophagy; D045744:Cell Line, Tumor; D049109:Cell Proliferation; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure; D005909:Glioblastoma / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D008819:Mice, Nude; D015398:Signal Transduction
chemical_list: C582104:EMC6 protein, human; D008565:Membrane Proteins