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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RIOK2_HUMAN RIOK2_HUMAN]] Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function (PubMed:21880710).<ref>PMID:16037817</ref> <ref>PMID:19564402</ref> <ref>PMID:21880710</ref> | [[http://www.uniprot.org/uniprot/RIOK2_HUMAN RIOK2_HUMAN]] Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function (PubMed:21880710).<ref>PMID:16037817</ref> <ref>PMID:19564402</ref> <ref>PMID:21880710</ref> | ||
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== Publication Abstract from PubMed == | |||
RIO proteins form a conserved family of atypical protein kinases. RIO2 is a serine/threonine protein kinase/ATPase involved in pre-40S ribosomal maturation. Current crystal structures of archaeal and fungal Rio2 proteins report a monomeric form of the protein. Here, we describe three atomic structures of the human RIO2 kinase showing that it forms a homodimer in vitro. Upon self-association, each protomer ATP-binding pocket is partially remodelled and found in an apostate. The homodimerization is mediated by key residues previously shown to be responsible for ATP binding and catalysis. This unusual in vitro protein kinase dimer reveals an intricate mechanism where identical residues are involved in substrate binding and oligomeric state formation. We speculate that such an oligomeric state might be formed also in vivo and might function in maintaining the protein in an inactive state and could be employed during import. | |||
In vitro dimerization of human RIO2 kinase.,Maurice F, Perebaskine N, Thore S, Fribourg S RNA Biol. 2019 Nov;16(11):1633-1642. doi: 10.1080/15476286.2019.1653679. Epub, 2019 Aug 14. PMID:31390939<ref>PMID:31390939</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
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Revision as of 09:02, 10 October 2019
Human Rio2 kinase structureHuman Rio2 kinase structure
Structural highlights
Function[RIOK2_HUMAN] Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function (PubMed:21880710).[1] [2] [3] Publication Abstract from PubMedRIO proteins form a conserved family of atypical protein kinases. RIO2 is a serine/threonine protein kinase/ATPase involved in pre-40S ribosomal maturation. Current crystal structures of archaeal and fungal Rio2 proteins report a monomeric form of the protein. Here, we describe three atomic structures of the human RIO2 kinase showing that it forms a homodimer in vitro. Upon self-association, each protomer ATP-binding pocket is partially remodelled and found in an apostate. The homodimerization is mediated by key residues previously shown to be responsible for ATP binding and catalysis. This unusual in vitro protein kinase dimer reveals an intricate mechanism where identical residues are involved in substrate binding and oligomeric state formation. We speculate that such an oligomeric state might be formed also in vivo and might function in maintaining the protein in an inactive state and could be employed during import. In vitro dimerization of human RIO2 kinase.,Maurice F, Perebaskine N, Thore S, Fribourg S RNA Biol. 2019 Nov;16(11):1633-1642. doi: 10.1080/15476286.2019.1653679. Epub, 2019 Aug 14. PMID:31390939[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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