TAILIEUCHUNG - báo cáo khoa hoc : Identification and characterization of novel spliced variants of PRMT2 in breast carcinoma

ProteinN-arginine methyltransferases (PRMTs) participate in a number of cellular processes, including cell growth, nuclear⁄cytoplasmic protein shut-tling, differentiation, RNA splicing and post-transcriptional regulation. PRMT2 (also known as HRMT1L1) is clearly involved in lung function, the inflammatory response | IFEBS Journal Identification and characterization of novel spliced variants of PRMT2 in breast carcinoma Jing Zhong1 2 Ren-Xian Cao1 2 Xu-Yu Zu1 Tao Hong1 2 Jing Yang1 2 Ling Liu1 Xin-Hua Xiao1 Wen-Jun Ding1 Qiang Zhao3 Jiang-Hua Liu1 and Ge-Bo Wen1 2 1 ClinicalMedicalResearch Institute of the First Affiliated Hospital University of South China Hengyang China 2 Department of Pathophysiology University of South China Hengyang China 3 Department of Pathology of the First Affiliated Hospital University of South China Hengyang China Keywords breast cancer ERa PRMT2 splice variants upregulated Correspondence Ge-Bo Wen ClinicalMedicalResearch Institute of the First Affiliated Hospital University of South China Hengyang 421001 China Fax 86 734 8279009 Tel 86 734 8279392 E-mail gb_wen@ These authors contributed equally to this work Received 19 August 2011 revised 31 October 2011 accepted 10 November 2011 doi Protein N-arginine methyltransferases PRMTs participate in a number of cellular processes including cell growth nuclear cytoplasmic protein shuttling differentiation RNA splicing and post-transcriptional regulation. PRMT2 also known as HRMT1L1 is clearly involved in lung function the inflammatory response apoptosis promotion Wnt signaling and leptin signaling regulation through different mechanisms. In this study we report the molecular and cell biological characterization of three novel PRMT2 splice variants isolated from breast cancer cells and referred to as PRMT2a PRMT2P and PRMT2y. Compared with the wild-type PRMT2 these variants lack different motifs and therefore generate distinct C-terminal domains. Confocal microscopy scanning revealed a distinct intracellular localization of PRMT2 variants suggesting that the alternatively spliced C-terminus of PRMT2 can directly influence its subcellular localization. Our findings reveal that these variants are capable of binding to estrogen receptor alpha ERa both in vitro and in

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