<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Lukoszek R</submitter><funding>Cancer Research UK</funding><funding>European Research Council</funding><funding>Medical Research Council</funding><funding>Royal Society</funding><funding>Wellcome Trust</funding><pagination>114405</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11290353</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>43(7)</volume><pubmed_abstract>The RNA cap methyltransferase CMTR1 methylates the first transcribed nucleotide of RNA polymerase II transcripts, impacting gene expression mechanisms, including during innate immune responses. Using mass spectrometry, we identify a multiply phosphorylated region of CMTR1 (phospho-patch [P-Patch]), which is a substrate for the kinase CK2 (casein kinase II). CMTR1 phosphorylation alters intramolecular interactions, increases recruitment to RNA polymerase II, and promotes RNA cap methylation. P-Patch phosphorylation occurs during the G1 phase of the cell cycle, recruiting CMTR1 to RNA polymerase II during a period of rapid transcription and RNA cap formation. CMTR1 phosphorylation is required for the expression of specific RNAs, including ribosomal protein gene transcripts, and promotes cell</pubmed_abstract><journal>Cell reports</journal><pubmed_title>CK2 phosphorylation of CMTR1 promotes RNA cap formation and influenza virus infection.</pubmed_title><pmcid>PMC11290353</pmcid><funding_grant_id>769080</funding_grant_id><funding_grant_id>097462/Z/11/Z</funding_grant_id><funding_grant_id>WRM\u2216R1\u2216180008</funding_grant_id><funding_grant_id>219416/A/19/Z</funding_grant_id><funding_grant_id>097945/Z/11/Z</funding_grant_id><funding_grant_id>CTRQQR-2021\u2216100006</funding_grant_id><funding_grant_id>A17196 / A31287</funding_grant_id><funding_grant_id>MR/K024213/1</funding_grant_id><pubmed_authors>Liang S</pubmed_authors><pubmed_authors>Brett NJM</pubmed_authors><pubmed_authors>Lukoszek R</pubmed_authors><pubmed_authors>Pirillo C</pubmed_authors><pubmed_authors>Inesta-Vaquera F</pubmed_authors><pubmed_authors>Cowling VH</pubmed_authors><pubmed_authors>Roberts EW</pubmed_authors><pubmed_authors>Hughes DJ</pubmed_authors><pubmed_authors>Hepburn LA</pubmed_authors></additional><is_claimable>false</is_claimable><name>CK2 phosphorylation of CMTR1 promotes RNA cap formation and influenza virus infection.</name><description>The RNA cap methyltransferase CMTR1 methylates the first transcribed nucleotide of RNA polymerase II transcripts, impacting gene expression mechanisms, including during innate immune responses. Using mass spectrometry, we identify a multiply phosphorylated region of CMTR1 (phospho-patch [P-Patch]), which is a substrate for the kinase CK2 (casein kinase II). CMTR1 phosphorylation alters intramolecular interactions, increases recruitment to RNA polymerase II, and promotes RNA cap methylation. P-Patch phosphorylation occurs during the G1 phase of the cell cycle, recruiting CMTR1 to RNA polymerase II during a period of rapid transcription and RNA cap formation. CMTR1 phosphorylation is required for the expression of specific RNAs, including ribosomal protein gene transcripts, and promotes cell</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Jul</publication><modification>2026-06-01T16:20:02.903Z</modification><creation>2025-04-19T07:05:25.057Z</creation></dates><accession>S-EPMC11290353</accession><cross_references><pubmed>38923463</pubmed><doi>10.1016/j.celrep.2024.114405</doi></cross_references></HashMap>