Methylarginines within the RGG-Motif Region of hnRNP A1 Affect Its IRES Trans-Acting Factor Activity and Are Required for hnRNP A1 Stress Granule Localization and Formation

详细信息    查看全文

• 作者：Michael L. Wall¹ ; Stephen M. Lewis¹ ; ² ; ³ ; ⁴ ; ^{stephenl@canceratl.ca}
• 关键词：Apaf-1 ; apoptotic protease activating factor 1 ; Bcl-xL ; B-cell lymphoma extra large ; CNBP ; cellular nucleic acid binding protein ; FGF2 ; fibroblast growth factor 2 ; G3BP1 ; Ras GTPase-activating protein-binding protein 1 ; IRES ; internal ribosome entry site ; ITAF ; internal ribosome entry site trans-acting factor ; JMJD6 ; jumonji domain containing 6 ; PRMT1 ; protein arginine methyltransferase 1 ; XIAP ; X-linked inhibitor of apoptosis ; hnRNP ; heterogeneous nuclear ribonucleoprotein ; RGG ; arginine&ndash
• 刊名：Journal of Molecular Biology
• 出版年：2017
• 出版时间：20 January 2017
• 年：2017
• 卷：429
• 期：2
• 页码：295-307
• 全文大小：1109 K
• 卷排序：429

文摘

The functional role of asymmetric dimethylation within the hnRNP A1 RGG-motif region is unknown. Lysine substitution within the RGG-motif region increases hnRNP A1 ITAF activity by 40%. Asymmetric dimethylation of hnRNP A1 may serve to inhibit ITAF activity. Alanine substitution within the RGG-motif region abolishes hnRNP A1 ITAF activity and mRNA-binding ability. The hnRNP A1 alanine mutant inhibits stress granule formation in a dominant-negative manner.