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Oncoprotein CIP 2A promotes the disassembly of primary cilia and inhibits glycolytic metabolism
Author(s) -
Jeong Ae Lee,
Ka Hye In,
Han Sora,
Lee Sunyi,
Lee EunWoo,
Soh Su Jung,
Joo Hyun Jeong,
Sumiyasuren Buyanravjkh,
Park Ji Young,
Lim JongSeok,
Park Jong Hoon,
Lee Myung Sok,
Yang Young
Publication year - 2018
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201745144
Subject(s) - cilium , microbiology and biotechnology , centrosome , biology , glycolysis , basal body , microtubule , protein phosphatase 2 , aurora a kinase , kinase , ciliogenesis , metabolism , chemistry , cell , cell cycle , biochemistry , phosphatase , phosphorylation , gene , flagellum
In most mammalian cells, the primary cilium is a microtubule‐enriched protrusion of the plasma membrane and acts as a key coordinator of signaling pathways during development and tissue homeostasis. The primary cilium is generated from the basal body, and cancerous inhibitor of protein phosphatase 2A ( CIP 2A), the overexpression of which stabilizes c‐ MYC to support the malignant growth of tumor cells, is localized in the centrosome. Here, we show that CIP 2A overexpression induces primary cilia disassembly through the activation of Aurora A kinase, and CIP 2A depletion increases ciliated cells and cilia length in retinal pigment epithelium ( RPE 1) cells. CIP 2A depletion also shifts metabolism toward the glycolytic pathway by altering the expression of metabolic genes related to glycolysis. However, glycolytic activation in CIP 2A‐depleted cells does not depend on cilia assembly, even though enhanced cilia assembly alone activates glycolytic metabolism. Collectively, these data suggest that CIP 2A promotes primary cilia disassembly and that CIP 2A depletion induces metabolic reprogramming independent of primary cilia.