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Literature summary for 2.1.1.319 extracted from

  • Hu, S.B.; Xiang, J.F.; Li, X.; Xu, Y.; Xue, W.; Huang, M.; Wong, C.C.; Sagum, C.A.; Bedford, M.T.; Yang, L.; Cheng, D.; Chen, L.L.
    Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus (2015), Genes Dev., 29, 630-645 .
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + [coiled-coil domain of p54nrb]-L-arginine Mus musculus the enzyme (CARM1) regulates this nuclear retention pathway at two levels: CARM1 methylates the coiled-coil domain of p54nrb, resulting in reduced binding of p54nrb to mRNAs containing inverted repeated Alu elements (IRAlus), and also acts as a transcription regulator to suppress NEAT1 transcription, leading to reduced paraspeckle formation. These actions of CARM1 work together synergistically to regulate the export of transcripts containing IRAlus from paraspeckles under certain cellular stresses, such as poly(I:C) treatment 2 S-adenosyl-L-homocysteine + [coiled-coil domain of p54nrb]-Nomega,Nomega-dimethyl-L-arginine
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 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9WVG6
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Source Tissue

Source Tissue Comment Organism Textmining
embryonic fibroblast
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 Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + [coiled-coil domain of p54nrb]-L-arginine
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 Mus musculus 2 S-adenosyl-L-homocysteine + [coiled-coil domain of p54nrb]-Nomega,Nomega-dimethyl-L-arginine
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 ?
2 S-adenosyl-L-methionine + [coiled-coil domain of p54nrb]-L-arginine the enzyme (CARM1) regulates this nuclear retention pathway at two levels: CARM1 methylates the coiled-coil domain of p54nrb, resulting in reduced binding of p54nrb to mRNAs containing inverted repeated Alu elements (IRAlus), and also acts as a transcription regulator to suppress NEAT1 transcription, leading to reduced paraspeckle formation. These actions of CARM1 work together synergistically to regulate the export of transcripts containing IRAlus from paraspeckles under certain cellular stresses, such as poly(I:C) treatment Mus musculus 2 S-adenosyl-L-homocysteine + [coiled-coil domain of p54nrb]-Nomega,Nomega-dimethyl-L-arginine
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 ?

Synonyms

Synonyms Comment Organism
CARM1
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 Mus musculus
coactivator-associated arginine methyltransferase 1
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 Mus musculus

General Information

General Information Comment Organism
malfunction disruption of CARM1 enhances the nuclear retention of mRNAs containing inverted repeated Alu elements (IRAlus) Mus musculus
physiological function the enzyme (CARM1) regulates this nuclear retention pathway at two levels: CARM1 methylates the coiled-coil domain of p54nrb, resulting in reduced binding of p54nrb to mRNAs containing inverted repeated Alu elements (IRAlus), and also acts as a transcription regulator to suppress NEAT1 transcription, leading to reduced paraspeckle formation. These actions of CARM1 work together synergistically to regulate the export of transcripts containing IRAlus from paraspeckles under certain cellular stresses, such as poly(I:C) treatment Mus musculus