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SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation.


ABSTRACT: The SAM domain and HD domain containing protein 1 (SAMHD1) inhibits retroviruses, DNA viruses and long interspersed element 1 (LINE-1). Given that in dividing cells, SAMHD1 loses its antiviral function yet still potently restricts LINE-1, we propose that, instead of blocking viral DNA synthesis by virtue of its dNTP triphosphohydrolase activity, SAMHD1 may exploit a different mechanism to control LINE-1. Here, we report a new activity of SAMHD1 in promoting cellular stress granule assembly, which correlates with increased phosphorylation of eIF2? and diminished eIF4A/eIF4G interaction. This function of SAMHD1 enhances sequestration of LINE-1 RNP in stress granules and consequent blockade to LINE-1 retrotransposition. In support of this new mechanism of action, depletion of stress granule marker proteins G3BP1 or TIA1 abrogates stress granule formation and overcomes SAMHD1 inhibition of LINE-1. Together, these data reveal a new mechanism for SAMHD1 to control LINE-1 by activating cellular stress granule pathway.

SUBMITTER: Hu S 

PROVIDER: S-EPMC4489885 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature

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SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation.

Hu Siqi S   Li Jian J   Xu Fengwen F   Mei Shan S   Le Duff Yann Y   Yin Lijuan L   Pang Xiaojing X   Cen Shan S   Jin Qi Q   Liang Chen C   Guo Fei F  

PLoS genetics 20150702 7


The SAM domain and HD domain containing protein 1 (SAMHD1) inhibits retroviruses, DNA viruses and long interspersed element 1 (LINE-1). Given that in dividing cells, SAMHD1 loses its antiviral function yet still potently restricts LINE-1, we propose that, instead of blocking viral DNA synthesis by virtue of its dNTP triphosphohydrolase activity, SAMHD1 may exploit a different mechanism to control LINE-1. Here, we report a new activity of SAMHD1 in promoting cellular stress granule assembly, whic  ...[more]

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