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Gene Review

CARM1  -  coactivator-associated arginine...

Homo sapiens

Synonyms: Coactivator-associated arginine methyltransferase 1, Histone-arginine methyltransferase CARM1, PRMT4, Protein arginine N-methyltransferase 4
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Disease relevance of CARM1

  • The staining intensity for CARM1 was significantly lower in benign prostate tissue specimens compared with PIN and prostatic adenocarcinoma specimens (P < 0.001) [1].
  • Expression of CARM1 was not correlated with age, Gleason score sum, pathologic stage, lymph node metastasis, extraprostatic extension, surgical margin status, vascular invasion, or perineural invasion [1].
  • METHODS: The expression of CARM1 in normal prostate epithelium, high-grade prostatic intraepithelial neoplasia (PIN), and prostate carcinoma tissue was examined in 66 previously untreated patients with prostate carcinomas, as well as 12 patients with hormone-independent prostate carcinoma, using immunohistochemical methods [1].
  • First, transfection studies demonstrated that overexpression of CARM1 wild-type protein resulted in increased Tax transactivation of the human T-cell lymphotropic virus type 1 (HTLV-1) long terminal repeat (LTR) [2].
  • The identification of splicing factors that are methylated by CARM1, and protein-protein interactions that are regulated by CARM1, strongly implicates this enzyme in the regulation of alternative splicing and points toward its involvement in spinal muscular atrophy pathogenesis [3].

High impact information on CARM1


Chemical compound and disease context of CARM1

  • In the 12 patients with androgen-independent prostatic adenocarcinoma, the expression of CARM1 was significantly increased when compared with patients without previous hormonal treatment [1].

Biological context of CARM1


Anatomical context of CARM1

  • Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development [11].
  • They also demonstrate for the first time that CARM1 occupancy, histone H3-R17 methylation, and citrullination are regulated at the promoters of inflammatory genes in monocytes, thereby suggesting a novel role for histone arginine modifications in inflammatory diseases [12].
  • CARM1 regulates proliferation of PC12 cells by methylating HuD [13].

Associations of CARM1 with chemical compounds


Physical interactions of CARM1


Regulatory relationships of CARM1

  • CARM1 synergizes with CIITA in activating MHC-II transcription and synergy is abrogated when an arginine methyltransferase-defective CARM1 mutant is used [10].
  • Together, our data provide evidence that CARM1 enhances Tax transactivation of the HTLV-1 LTR through a direct interaction between CARM1 and Tax and this binding promotes methylation of histone H3 (R2, R17, and R26) [2].

Other interactions of CARM1


Analytical, diagnostic and therapeutic context of CARM1


  1. Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status. Hong, H., Kao, C., Jeng, M.H., Eble, J.N., Koch, M.O., Gardner, T.A., Zhang, S., Li, L., Pan, C.X., Hu, Z., MacLennan, G.T., Cheng, L. Cancer (2004) [Pubmed]
  2. Coactivator-Associated Arginine Methyltransferase 1 Enhances Transcriptional Activity of the Human T-Cell Lymphotropic Virus Type 1 Long Terminal Repeat through Direct Interaction with Tax. Jeong, S.J., Lu, H., Cho, W.K., Park, H.U., Pise-Masison, C., Brady, J.N. J. Virol. (2006) [Pubmed]
  3. The Arginine Methyltransferase CARM1 Regulates the Coupling of Transcription and mRNA Processing. Cheng, D., C??t??, J., Shaaban, S., Bedford, M.T. Mol. Cell (2007) [Pubmed]
  4. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. An, W., Kim, J., Roeder, R.G. Cell (2004) [Pubmed]
  5. Histone deimination antagonizes arginine methylation. Cuthbert, G.L., Daujat, S., Snowden, A.W., Erdjument-Bromage, H., Hagiwara, T., Yamada, M., Schneider, R., Gregory, P.D., Tempst, P., Bannister, A.J., Kouzarides, T. Cell (2004) [Pubmed]
  6. Regulation of transcription by a protein methyltransferase. Chen, D., Ma, H., Hong, H., Koh, S.S., Huang, S.M., Schurter, B.T., Aswad, D.W., Stallcup, M.R. Science (1999) [Pubmed]
  7. A methylation-mediator complex in hormone signaling. Xu, W., Cho, H., Kadam, S., Banayo, E.M., Anderson, S., Yates, J.R., Emerson, B.M., Evans, R.M. Genes Dev. (2004) [Pubmed]
  8. Control of CBP co-activating activity by arginine methylation. Chevillard-Briet, M., Trouche, D., Vandel, L. EMBO J. (2002) [Pubmed]
  9. Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression. Covic, M., Hassa, P.O., Saccani, S., Buerki, C., Meier, N.I., Lombardi, C., Imhof, R., Bedford, M.T., Natoli, G., Hottiger, M.O. EMBO J. (2005) [Pubmed]
  10. Interplay among coactivator-associated arginine methyltransferase 1, CBP, and CIITA in IFN-gamma-inducible MHC-II gene expression. Zika, E., Fauquier, L., Vandel, L., Ting, J.P. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  11. Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development. Kim, J., Lee, J., Yadav, N., Wu, Q., Carter, C., Richard, S., Richie, E., Bedford, M.T. J. Biol. Chem. (2004) [Pubmed]
  12. Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17. Miao, F., Li, S., Chavez, V., Lanting, L., Natarajan, R. Mol. Endocrinol. (2006) [Pubmed]
  13. CARM1 regulates proliferation of PC12 cells by methylating HuD. Fujiwara, T., Mori, Y., Chu, D.L., Koyama, Y., Miyata, S., Tanaka, H., Yachi, K., Kubo, T., Yoshikawa, H., Tohyama, M. Mol. Cell. Biol. (2006) [Pubmed]
  14. Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase. Li, H., Park, S., Kilburn, B., Jelinek, M.A., Henschen-Edman, A., Aswad, D.W., Stallcup, M.R., Laird-Offringa, I.A. J. Biol. Chem. (2002) [Pubmed]
  15. Signal-dependent control of gluconeogenic key enzyme genes through coactivator-associated arginine methyltransferase 1. Krones-Herzig, A., Mesaros, A., Metzger, D., Ziegler, A., Lemke, U., Brüning, J.C., Herzig, S. J. Biol. Chem. (2006) [Pubmed]
  16. The activity and stability of the transcriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation. Naeem, H., Cheng, D., Zhao, Q., Underhill, C., Tini, M., Bedford, M.T., Torchia, J. Mol. Cell. Biol. (2007) [Pubmed]
  17. Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter. Ma, H., Baumann, C.T., Li, H., Strahl, B.D., Rice, R., Jelinek, M.A., Aswad, D.W., Allis, C.D., Hager, G.L., Stallcup, M.R. Curr. Biol. (2001) [Pubmed]
  18. SNF2-related CBP activator protein (SRCAP) functions as a coactivator of steroid receptor-mediated transcription through synergistic interactions with CARM-1 and GRIP-1. Monroy, M.A., Schott, N.M., Cox, L., Chen, J.D., Ruh, M., Chrivia, J.C. Mol. Endocrinol. (2003) [Pubmed]
  19. Signaling within a Coactivator Complex: Methylation of SRC-3/AIB1 Is a Molecular Switch for Complex Disassembly. Feng, Q., Yi, P., Wong, J., O'malley, B.W. Mol. Cell. Biol. (2006) [Pubmed]
  20. Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity. Lee, Y.H., Campbell, H.D., Stallcup, M.R. Mol. Cell. Biol. (2004) [Pubmed]
  21. Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function. Teyssier, C., Chen, D., Stallcup, M.R. J. Biol. Chem. (2002) [Pubmed]
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