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Gene Review:

PRMT2 - protein arginine methyltransferase 2

Homo sapiens

Synonyms: HMT1, HRMT1L1, Histone-arginine N-methyltransferase PRMT2, MGC111373, Protein arginine N-methyltransferase 2

Kzhyshkowska, J. et al., Ortiz, D.F. et al., Qi, C. et al., Yoshimoto, T. et al., Ganesh, L. et al., et al.

Kzhyshkowska, Schütt, Liss, Kremmer, Stauber, Wolf, Dobner,

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Disease relevance of PRMT2

These results demonstrate that PRMTs are expressed and functional in the lung, and that hypoxia is a potent regulator of PRMT2 expression and lung ADMA concentrations [1].

High impact information on PRMT2

Analysis of fractionated fission yeast cell components indicates that the HMT1 polypeptide is associated with the vacuolar membrane [2].
Additionally, fission yeast strains harboring an hmt1-expressing multicopy plasmid exhibit enhanced metal tolerance along with a higher intracellular level of cadmium, implying a relationship between HMT1 mediated transport and compartmentalization of heavy metals [2].
Mouse embryo fibroblasts from PRMT2 genetic knockouts showed elevated NF-kappaB activity and decreased susceptibility to apoptosis compared to wild-type or complemented cells [3].
The highly conserved S-adenosylmethionine-binding domain of PRMT2 mediated this effect [3].
In addition, PRMT2 enhanced PR, PPARgamma, and RARalpha-mediated transactivation [4].

Biological context of PRMT2

HRMT1L3 is a PRMT1 paralogue with highly conserved sequences and exact exon junctions, whereas the PRMT2 orthologues are very diverged [5].
The Src homology 3 (SH3) domain of HRMT1L1 was essential for its interaction with E1B-AP5 in vivo [6].
We suggest that HRMT1L1 is responsible for specific E1B-AP5 methylation in vivo [6].
HRMT1L1 maps to a YAC containing the telomere of chromosome 21q [7].

Associations of PRMT2 with chemical compounds

PRMT2 enhanced both ERalpha AF-1 and AF-2 transcriptional activity, and the potential methyltransferase activity of PRMT2 appeared pivotal for its coactivator function [4].
The arginine methyltransferase PRMT2 binds RB and regulates E2F function [8].

Physical interactions of PRMT2

Using yeast two-hybrid screening we identified HRMT1L1 (PRMT2) as one of the proteins interacting with E1B-AP5 [6].

Co-localisations of PRMT2

By in situ immunofluorescence we demonstrated that E1B-AP5 co-localizes with the nuclear fraction of HRMT1L1 [6].

Other interactions of PRMT2

Vascular injury to PRMT2(-/-) arteries results in a hyperplastic response, consistent with increased G1-S phase progression [8].
Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha [4].

Analytical, diagnostic and therapeutic context of PRMT2

To further explore the role of endogenous PRMT2 in the regulation of E2F activity, the PRMT2 gene was ablated in mice by gene targeting [8].

References

Increased protein arginine methylation in chronic hypoxia: role of protein arginine methyltransferases. Yildirim, A.O., Bulau, P., Zakrzewicz, D., Kitowska, K.E., Weissmann, N., Grimminger, F., Morty, R.E., Eickelberg, O. Am. J. Respir. Cell Mol. Biol. (2006) [Pubmed]
Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter. Ortiz, D.F., Kreppel, L., Speiser, D.M., Scheel, G., McDonald, G., Ow, D.W. EMBO J. (1992) [Pubmed]
Protein Methyltransferase 2 Inhibits NF-{kappa}B Function and Promotes Apoptosis. Ganesh, L., Yoshimoto, T., Moorthy, N.C., Akahata, W., Boehm, M., Nabel, E.G., Nabel, G.J. Mol. Cell. Biol. (2006) [Pubmed]
Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. Qi, C., Chang, J., Zhu, Y., Yeldandi, A.V., Rao, S.M., Zhu, Y.J. J. Biol. Chem. (2002) [Pubmed]
Identification and phylogenetic analyses of the protein arginine methyltransferase gene family in fish and ascidians. Hung, C.M., Li, C. Gene (2004) [Pubmed]
Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1. Kzhyshkowska, J., Schütt, H., Liss, M., Kremmer, E., Stauber, R., Wolf, H., Dobner, T. Biochem. J. (2001) [Pubmed]
Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Scott, H.S., Antonarakis, S.E., Lalioti, M.D., Rossier, C., Silver, P.A., Henry, M.F. Genomics (1998) [Pubmed]
The arginine methyltransferase PRMT2 binds RB and regulates E2F function. Yoshimoto, T., Boehm, M., Olive, M., Crook, M.F., San, H., Langenickel, T., Nabel, E.G. Exp. Cell Res. (2006) [Pubmed]

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