TAILIEUCHUNG - Báo cáo khoa học: Modulation of glucocorticoid receptor-interacting protein 1 (GRIP1) transactivation and co-activation activities through its C-terminal repression and self-association domains

Glucocorticoid receptor-interacting protein 1 (GRIP1), a p160 family nuc-lear receptor co-activator, possesses at least two autonomous activation domains (AD1 andAD2) in the C-terminal activity appears to be mediated by CBP⁄p300, whereasAD2 activity is apparently mediated through co-activator-associated arginine methyltransferase 1 (CARM1). | iFEBS Journal Modulation of glucocorticoid receptor-interacting protein 1 GRIP1 transactivation and co-activation activities through its C-terminal repression and self-association domains Pei-Yao Liu1 Tsai-Yuan Hsieh2 Wei-Yuan Chou1 and Shih-Ming Huang1 1 Department of Biochemistry NationalDefense MedicalCenter Taipei Taiwan 2 Department of Medicine Division of Gastroenterology Tri-Service General Hospital NationalDefense MedicalCenter Taipei Taiwan Keywords co-activation GRIP1 HDAC1 nuclear receptor transactivation Correspondence . Huang NationalDefense Medical Center Department of Biochemistry 161 Section 6 MinChuan East Road Taipei Taiwan 114 Fax 886 287924057 Tel 886 227937318 E-mail shihming@ Received 11 December 2005 revised 13 March 2006 accepted 16 March 2006 doi Glucocorticoid receptor-interacting protein 1 GRIP1 a p160 family nuclear receptor co-activator possesses at least two autonomous activation domains AD1 and AD2 in the C-terminal region. AD1 activity appears to be mediated by CBP p300 whereas AD2 activity is apparently mediated through co-activator-associated arginine methyltransferase 1 CARM1 . The mechanisms responsible for regulating the activities of AD1 and AD2 are not well understood. We provide evidence that the GRIP1 C-terminal region may be involved in regulating its own transactivation and nuclear receptor co-activation activities through primary self-association and a repression domain. We also compared the effects of the GRIP1 C terminus with those of other factors that functionally interact with the GRIP1 C terminus such as CARM1. Based on our results we propose a regulatory mechanism involving conformational changes to GRIP1 mediated through its intramolecular and intermolecular interactions and through modulation of the effects of co-repressors on its repression domains. These are the first results to indicate that the structural components of GRIP1 especially those of the C .

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