Physical and functional interactions between hnRNP K and PRMT family proteins

Chan, James Yi-Hsin; Hsieh, Tsai-Yuan; Liu, Shu-Ting; Chou, Wei-Yuan; Chung, Min-Huey; Huang, Shih-Ming

doi:10.1016/j.febslet.2008.12.025

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Volume 583, Issue 2 , Pages 281-286, 22 January 2009

Physical and functional interactions between hnRNP K and PRMT family proteins

Edited by Ivan Sadowski

James Yi-Hsin Chan
- Graduate Institute of Medical Sciences, National Defense Medical Center, Room 7102, 161, Section 6, MinChuan, Taipei 114, Taiwan, ROC
Tsai-Yuan Hsieh
- Division of Gastroenterology, Department of Internal Medicine, Tri-Service General Hospital, National Defense Medical Center, Taipei 114, Taiwan, ROC
Shu-Ting Liu
- Graduate Institute of Medical Sciences, National Defense Medical Center, Room 7102, 161, Section 6, MinChuan, Taipei 114, Taiwan, ROC
Wei-Yuan Chou
- Department of Biochemistry, National Defense Medical Center, Taipei 114, Taiwan, ROC
Min-Huey Chung
- Graduate Institute of Nursing, College of Nursing, Taipei Medical University, Taipei 110, Taiwan, ROC
Shih-Ming Huang
- Graduate Institute of Medical Sciences, National Defense Medical Center, Room 7102, 161, Section 6, MinChuan, Taipei 114, Taiwan, ROC
- Department of Biochemistry, National Defense Medical Center, Taipei 114, Taiwan, ROC
- Corresponding author. Address: Graduate Institute of Medical Sciences, National Defense Medical Center, Room 7102, 161, Section 6, MinChuan, Taipei 114, Taiwan, ROC. Fax: +886 2 87923106.

Received 21 October 2008; received in revised form 3 December 2008; accepted 10 December 2008. published online 19 December 2008.

Abstract

The mechanism underlying the protein–protein interaction of hnRNP K and PRMT family proteins is unclear. We examined and confirmed the arginine methylation of hnRNP K protein by PRMT1, not CARM1, via their direct binding. We also studied hnRNP K protein complexes containing CARM1, as well as PRMT1, using co-immunoprecipitation analysis. PRMT family proteins might be involved in the regulation of hnRNP K functions in nuclear receptor coactivator, transactivation, and p21 gene and protein expressions. We believe these observations will help provide insights into the regulation of hnRNP K protein functions via the recruitment of its associated proteins, including its arginine methylation-modifying proteins.

Structured summary

MINT-6803853: hnRPK, (uniprotkb:P61978) binds (MI:0407) to PRMT1 (uniprotkb:Q99873) by pull down (MI:0096)

MINT-6803884: hnRPK, (uniprotkb:P61978) physically interacts (MI:0218) with CARM1 (uniprotkb:Q86X55) by anti tag coimmunoprecipitation (MI:0007)

MINT-6803869: hnRPK, (uniprotkb:P61978) physically interacts (MI:0218) with PRMT1 (uniprotkb:Q99873) by anti tag coimmunoprecipitation (MI:0007)

MINT-6803939: hnRPK, (uniprotkb:P61978) binds (MI:0407) to PRMT2 (uniprotkb:P55345) by pull down (MI:0096)

MINT-6803929: hnRPK, (uniprotkb:P61978) binds (MI:0407) to RMT (uniprotkb:P38074) by pull down (MI:0096)

MINT-6803896: hnRPK, (uniprotkb:P61978) binds (MI:0407) to PRMT3 (uniprotkb:O60678) by pull down (MI:0096)

MINT-6803834: PRMT1 (uniprotkb:Q99873) methylates (MI:0213) hnRPK, (uniprotkb:P61978) by methyltransferase assay (MI:0515)

Keywords: hnRNP K, PRMT, HCV Core protein, Protein–protein interaction