TAILIEUCHUNG - Báo cáo khoa học: The four and a half LIM domain protein 2 interacts with and regulates the HERG channel

Protein–protein interactions are critical for protein trafficking, localization and the regulation of ion channels. Thehuman ether-a-go-go-related gene (herg) encodes the a-subunit of the potassium channel underlying the rapid component of the cardiac delayed rectifier current. | ỊFEBS Journal The four and a half LIM domain protein 2 interacts with and regulates the HERG channel Jijin Lin1 Shuguang Lin1 Xiyong Yu1 Patrick C. Choy2 Xiuzhang Shen3 Chunyu Deng1 Sujuan Kuang1 and Jun Wu3 1 Department of Cardiology Guangdong ProvincialPeople s Hospital Guangdong ProvincialCardiovascular Institute China 2 Department of Biochemistry and MedicalGenetics Faculty of Medicine University of Manitoba Winnipeg Canada 3 Department of Cardiology The First Affiliated Hospital Shantou University MedicalCollege China Keywords FHL2 HERG long-QT syndrome potassium channel protein-protein interaction Correspondence S. Lin Department of Cardiology Guangdong ProvincialPeople s Hospital Guangdong ProvincialCardiovascular Institute 96 Dongchuan Road Guangzhou 510080 China Fax 86 20 838 27712 Tel 86 20 838 27812 21180 E-mail shuguanglin@ Received 23 May 2008 revised 9 July 2008 accepted 11 July 2008 doi Protein-protein interactions are critical for protein trafficking localization and the regulation of ion channels. The human ether-a-go-go-related gene herg encodes the a-subunit of the potassium channel underlying the rapid component of the cardiac delayed rectifier current. To identify the cellular proteins involved in the regulation of the HERG channel a human heart cDNA library was screened using a yeast two-hybrid system with the N-terminus of HERG as bait. The four and a half LIM domain protein 2 FHL2 was identified as a potential HERG partner. The interaction between these two proteins was confirmed by co-immunoprecipitation and glutathione transferase pull-down assays and immunocytochemical analysis. The physiological implication of HERG-FHL2 interaction assessed by whole-cell patch-clamp electrophysiology experiments showed a significant increase in the HERG current amplitude and a faster deactivation of the tail current in human embryonic kidney 293 cells co-expressing HERG and FHL2. These data indicate that FHL2 .

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