Priority Research Papers:

PRMT1 promotes mitosis of cancer cells through arginine methylation of INCENP

Xiaolan Deng _, Gottfried Von Keudell, Takehiro Suzuki, Naoshi Dohmae, Makoto Nakakido, Lianhua Piao, Yuichiro Yoshioka, Yusuke Nakamura and Ryuji Hamamoto

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Oncotarget. 2015; 6:35173-35182. https://doi.org/10.18632/oncotarget.6050

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Xiaolan Deng1,2, Gottfried Von Keudell1, Takehiro Suzuki3, Naoshi Dohmae3, Makoto Nakakido1, Lianhua Piao1, Yuichiro Yoshioka1, Yusuke Nakamura1 and Ryuji Hamamoto1

1 Section of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL, USA

2 Department of Pharmaceutical Analysis, School of Pharmacy, China Medical University, Shenyang, P. R. China

3 Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Saitama, Japan

Correspondence to:

Ryuji Hamamoto, email:

Keywords: INCENP, Aurora kinase B, PRMT1, arginine methylation

Received: August 20, 2015 Accepted: September 25, 2015 Published: October 09, 2015


Inner centromere protein (INCENP) is a part of a protein complex known as the chromosomal passenger complex (CPC) that is essential for correcting non-bipolar chromosome attachments and for cytokinesis. We here demonstrate that a protein arginine methyltransferase PRMT1, which are overexpressed in various types of cancer including lung and bladder cancer, methylates arginine 887 in an Aurora Kinase B (AURKB)-binding region of INCENP both in vitro and in vivo. R887-substituted INCENP revealed lower binding-affinity to AURKB than wild-type INCENP in the presence of PRMT1. Knockdown of PRMT1 as well as overexpression of methylation-inactive INCENP attenuated the AURKB activity in cancer cells, and resulted in abnormal chromosomal alignment and segregation. Furthermore, introduction of methylation-inactive INCENP into cancer cells reduced the growth rate, compared with those introduced wild-type INCENP or Mock. Our data unveils a novel mechanism of PRMT1-mediated CPC regulation through methylation of INCENP.

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