Sung-Hyun Kim

University of Minnesota

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Ann M. Bode

Royal Belfast Hospital for Sick Children

Dong Hoon Yu

First Affiliated Hospital of Jinan University

Yong‐Yeon Cho

Catholic University of Korea

Ke Yao

Henan Tianguan Group (China)

Zigang Dong

China-US (Henan) Hormel Cancer Institute

Hanyong Chen

Hormel (United States)

Sungyoung Lee

Seoul National University

Ki Beom Bae

Inje University Busan Paik Hospital

Myoung Ok Kim

Kyungpook National University

Kun-Yeong Lee

University of Minnesota

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University of Minnesota

Hormel (United States)

Seoul National University

Zhengzhou University

Kyungpook National University

China-US (Henan) Hormel Cancer Institute

Kyung Hee University

Catholic University of Korea

Advanced Institute of Convergence Technology

Korea Research Institute of Bioscience and Biotechnology

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ERK1 phosphorylates Nanog to regulate protein stability and stem cell self-renewal

Stem Cell Research (2014)

Sung-Hyun Kim Myoung Ok Kim Yong‐Yeon Cho Ke Yao Dong Joon Kim

Nanog regulates human and mouse embryonic stem (ES) cell self-renewal activity. Activation of ERKs signaling negatively regulates ES cell self-renewal and induces differentiation, but the mechanisms are not understood. We found that ERK1 binds and phosphorylates Nanog. Activation of MEK/ERKs signaling and phosphorylation of Nanog inhibit Nanog transactivation, inducing ES cell differentiation. Conversely, suppression of MEK/ERKs signaling enhances Nanog transactivation to inhibit ES cell differentiation. We observed that phosphorylation of Nanog by ERK1 decreases Nanog stability through ubiquitination-mediated protein degradation. Further, we found that this phosphorylation induces binding of FBXW8 with Nanog to reduce Nanog protein stability. Overall, our results demonstrated that ERKs-mediated Nanog phosphorylation plays an important role in self-renewal of ES cells through FBXW8-mediated Nanog protein stability.

Homeobox protein NANOG

Nanog Homeobox Protein

Rex1

10.1016/j.scr.2014.04.001

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JNK1 and 2 play a negative role in reprogramming to pluripotent stem cells by suppressing Klf4 activity

Stem Cell Research (2013)

Ke Yao Myoung Ok Ki Hanyong Chen Yong‐Yeon Cho Sung-Hyun Kim

Embryonic stem (ES) cells are pluripotent cells with the capacity for unlimited self-renewal or differentiation. Inhibition of MAPK pathways enhances mouse ES cell pluripotency characteristics. Compared to wildtype ES cells, jnk2(-/-) ES cells displayed a much higher growth rate. To determine whether JNKs are required for stem cell self-renewal or differentiation, we performed a phosphorylation kinase array assay to compare mouse ES cells under LIF+ or LIF- culture conditions. The data showed that activation of JNKs was induced by LIF withdrawal. We also found that JNK1 or 2 phosphorylated Klf4 at threonines 224 and 225. Activation of JNK signaling and phosphorylation of Klf4 inhibited Klf4 transcription and transactivation activity. Importantly, jnk1(-/-) and jnk2(-/-) murine embryonic fibroblasts (MEFs) exhibited a significantly greater potency in the ability to increase the number of iPS colonies compared with jnk wildtype MEFs. Overall, our results demonstrated that JNK1 and 2 play a negative role in reprogramming to pluripotent stem cells by suppressing Klf4 activity.

Reprogramming

KLF4

10.1016/j.scr.2013.10.005

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Citations (24)