Priority Research Papers:
PRMT1 promotes mitosis of cancer cells through arginine methylation of INCENP
PDF | HTML | Supplementary Files | How to cite
Metrics: PDF 2539 views | HTML 3122 views | ?
Abstract
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
Abstract
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.
All site content, except where otherwise noted, is licensed under a Creative Commons Attribution 4.0 License.
PII: 6050