Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (CMTR1)

CMTR1 is an S-adenosylmethionine-dependent methyltransferase, part of the RNA capping machinery, that adds a methyl group to the ribose of the first nucleotide of eukaryotic mRNA (producing cap1 structure, m7GpppNm)[3][2][1]. This modification is essential for: - mRNA splicing, export, and translation - Protection from exonucleases - Recruitment of cap-binding proteins (CBC, eIF4F, eIF4E) - Preventing activation of innate immune sensors (RIG-I, MDA5, IFIT) by self-RNA CMTR1 is genetically regulated, upregulated during differentiation (notably in neural tissues)[1][4], and its deficiency triggers immune response activation, mimicking viral infection signaling[3]. It is a multi-domain nuclear protein interacting with RNA polymerase II and other cap-processing machinery members. The enzyme has a recognized role in distinguishing self versus non-self RNAs, thereby controlling the balance between normal cell function and antiviral response[3][2][1]. No small-molecule drugs targeting CMTR1 are currently described, but its role in immune system signaling and RNA biology suggests potential as a therapeutic target for antiviral, cancer, or immunomodulatory strategies. Knockout or mutation can lead to defective cell proliferation, neurological defects, or altered immune responses[4][1][3].

Other names

FTSJD2KIAA0082MTR1MTr1hMTr1ISG95Cap1 2'O-ribose methyltransferase 1FtsJ methyltransferase domain-containing protein 2Interferon-stimulated gene 95 kDa proteinS-adenosyl-L-methionine-dependent methyltransferase FTSJD2cap1 2'O-ribose methyltransferase 1

Inhibition or modulation of 2′-O-methyltransferase activity to influence immune recognition of RNA. Potential indirect immune modulation (through interferon response signaling).