Endosomal phosphatidylserine is critical for the YAP signalling pathway in proliferating cells

Tatsuyuki Matsudaira, Kojiro Mukai, Taishin Noguchi, Junya Hasegawa, Tomohisa Hatta, Shun-ichiro Iemura, Tohru Natsume, Norio Miyamura, Hiroshi Nishina, Jun Nakayama, Kentaro Semba, Takuya Tomita, Shigeo Murata, Hiroyuki Arai () and Tomohiko Taguchi ()
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Tatsuyuki Matsudaira: University of Tokyo
Kojiro Mukai: University of Tokyo
Taishin Noguchi: University of Tokyo
Junya Hasegawa: University of Tokyo
Tomohisa Hatta: National Institute of Advanced Industrial Science and Technology
Shun-ichiro Iemura: Fukushima Medical University
Tohru Natsume: National Institute of Advanced Industrial Science and Technology
Norio Miyamura: Tokyo Medical and Dental University
Hiroshi Nishina: Tokyo Medical and Dental University
Jun Nakayama: Waseda University
Kentaro Semba: Waseda University
Takuya Tomita: The University of Tokyo
Shigeo Murata: The University of Tokyo
Hiroyuki Arai: University of Tokyo
Tomohiko Taguchi: University of Tokyo

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract Yes-associated protein (YAP) is a recently discovered growth-promoting transcription coactivator that has been shown to regulate the malignancy of various cancers. How YAP is regulated is not fully understood. Here, we show that one of the factors regulating YAP is phosphatidylserine (PS) in recycling endosomes (REs). We use proximity biotinylation to find proteins proximal to PS. Among these proteins are YAP and multiple proteins related to YAP signalling. Knockdown of ATP8A1 (an RE PS-flippase) or evectin-2 (an RE-resident protein) and masking of PS in the cytoplasmic leaflet of membranes, all suppress nuclear localization of YAP and YAP-dependent transcription. ATP8A1 knockdown increases the phosphorylated (activated) form of Lats1 that phosphorylates and inactivates YAP, whereas evectin-2 knockdown reduces the ubiquitination and increased the level of Lats1. The proliferation of YAP-dependent metastatic cancer cells is suppressed by knockdown of ATP8A1 or evectin-2. These results suggest a link between a membrane phospholipid and cell proliferation.

Date: 2017
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DOI: 10.1038/s41467-017-01255-3

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