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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00002534naa a2200337 4500
001oai:prod.swepub.kib.ki.se:146995746
003SwePub
008240913s2021 | |||||||||||000 ||eng|
024a http://kipublications.ki.se/Default.aspx?queryparsed=id:1469957462 URI
024a https://doi.org/10.3390/ijms221262872 DOI
040 a (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Reuper, H4 aut
2451 0a Arabidopsis thaliana G3BP Ortholog Rescues Mammalian Stress Granule Phenotype across Kingdoms
264 c 2021-06-11
264 1b MDPI AG,c 2021
520 a Stress granules (SGs) are dynamic RNA–protein complexes localized in the cytoplasm that rapidly form under stress conditions and disperse when normal conditions are restored. The formation of SGs depends on the Ras-GAP SH3 domain-binding protein (G3BP). Formations, interactions and functions of plant and human SGs are strikingly similar, suggesting a conserved mechanism. However, functional analyses of plant G3BPs are missing. Thus, members of the Arabidopsis thaliana G3BP (AtG3BP) protein family were investigated in a complementation assay in a human G3BP knock-out cell line. It was shown that two out of seven AtG3BPs were able to complement the function of their human homolog. GFP-AtG3BP fusion proteins co-localized with human SG marker proteins Caprin-1 and eIF4G1 and restored SG formation in G3BP double KO cells. Interaction between AtG3BP-1 and -7 and known human G3BP interaction partners such as Caprin-1 and USP10 was also demonstrated by co-immunoprecipitation. In addition, an RG/RGG domain exchange from Arabidopsis G3BP into the human G3BP background showed the ability for complementation. In summary, our results support a conserved mechanism of SG function over the kingdoms, which will help to further elucidate the biological function of the Arabidopsis G3BP protein family.
700a Gotte, B4 aut
700a Williams, L4 aut
700a Tan, TJC4 aut
700a McInerney, GMu Karolinska Institutet4 aut
700a Panas, MDu Karolinska Institutet4 aut
700a Krenz, B4 aut
710a Karolinska Institutet4 org
773t International journal of molecular sciencesd : MDPI AGg 22:12q 22:12x 1422-0067
856u https://doi.org/10.3390/ijms22126287
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:146995746
8564 8u https://doi.org/10.3390/ijms22126287

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