ORCID Profile
0000-0003-2963-4501
Current Organisations
Hiroshima University Hospital
,
Keio University
,
University of Cincinnati College of Medicine
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Publisher: Elsevier BV
Date: 03-2012
Publisher: BMJ
Date: 02-2006
Publisher: The Company of Biologists
Date: 2019
DOI: 10.1242/JCS.231886
Abstract: Ras proteins are small GTPases localized to the plasma membrane (PM), which regulate cellular proliferation, apoptosis and differentiation. After a series of posttranslational modifications, H- and N-Ras traffic to the PM from the Golgi via the classical exocytic pathway, but the exact mechanism of K-Ras trafficking to the PM from the ER is not fully characterized. ATP5G1 is one of the three proteins that compose subunit c of the F0 complex of the mitochondrial ATP synthase. In this study, we show that overexpression of the mitochondrial targeting sequence of ATP5G1 perturbs glucose metabolism, inhibits oncogenic K-Ras signaling, and redistributes phosphatidylserine (PtdSer) to mitochondria and other endomembranes, resulting in K-Ras translocation to mitochondria. Also, it depletes phosphatidylinositol (PI) 4-phosphate (P) at the Golgi. Glucose supplementation restores PtdSer and K-Ras PM localization and PI4P at the Golgi. We further show that inhibition of the Golgi-localized PI4-kinases (PI4Ks) translocates K-Ras, and PtdSer to mitochondria and endomembranes, respectively. We conclude that PI4P at the Golgi regulates the PM localization of PtdSer and K-Ras.
Location: United States of America
Location: United States of America
No related grants have been discovered for Atsuo Sasaki.