ULK1 phosphorylates Exo70 to suppress breast cancer metastasis

Liyuan Mao, Yan-yan Zhan (), Bin Wu, Qiang Yu, Liang Xu, Xiaoting Hong, Linhai Zhong, Panying Mi, Li Xiao, Xinquan Wang, Hanwei Cao, Wenqing Zhang, Binbin Chen, Jingzhou Xiang, Kunrong Mei, Ravi Radhakrishnan, Wei Guo () and Tianhui Hu ()
Additional contact information
Liyuan Mao: Xiamen University
Yan-yan Zhan: Xiamen University
Bin Wu: University of Pennsylvania
Qiang Yu: Xiamen University
Liang Xu: Xiamen University
Xiaoting Hong: Xiamen University
Linhai Zhong: Xiamen University
Panying Mi: Xiamen University
Li Xiao: Xiamen University
Xinquan Wang: Tsinghua University
Hanwei Cao: Xiamen University
Wenqing Zhang: Xiamen University
Binbin Chen: Xiamen University
Jingzhou Xiang: Xiamen University
Kunrong Mei: Tianjin University
Ravi Radhakrishnan: University of Pennsylvania
Wei Guo: University of Pennsylvania
Tianhui Hu: Xiamen University

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract Increased expression of protein kinase ULK1 was reported to negatively correlate with breast cancer metastasis. Here we report that ULK1 suppresses the migration and invasion of human breast cancer cells. The suppressive effect is mediated through direct phosphorylation of Exo70, a key component of the exocyst complex. ULK1 phosphorylation inhibits Exo70 homo-oligomerization as well as its assembly to the exocyst complex, which are needed for cell protrusion formation and matrix metalloproteinases secretion during cell invasion. Reversely, upon growth factor stimulation, Exo70 is phosphorylated by ERK1/2, which in turn suppresses its phosphorylation by ULK1. Together, our study identifies Exo70 as a substrate of ULK1 that inhibits cancer metastasis, and demonstrates that two counteractive regulatory mechanisms are well orchestrated during tumor cell invasion.

Date: 2020
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DOI: 10.1038/s41467-019-13923-7

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