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MRFAP1  -  Morf4 family associated protein 1

Homo sapiens

Synonyms: MORF4 family-associated protein 1, PAM14, PGR1, Protein PGR1, Protein associated with MRG of 14 kDa
 
 
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Disease relevance of MRFAP1

  • The C-terminal part of MRG15 forms a conserved MRG domain which is involved in interactions with the tumor suppressor protein retinoblastoma and a nucleoprotein PAM14 during transcriptional regulation [1].
 

High impact information on MRFAP1

  • These data demonstrate that PAM14 is not essential for normal mouse development and cell cycle control [2].
  • Pam14 was widely expressed in all mouse tissues and as early as 7 days during embryonic development [2].
  • Collectively these results suggest that MRG15 regulates transcription through interactions with a cellular protein complex containing Rb and PAM14 [3].
  • Site-directed mutagenesis studies based on the X-ray structure and bioinformatics identified key residues involved in the binding of PAM14 and MRGBP [4].
  • For the transcripts of sAPx and Csd2 high correlations with the calculated redox state of NADPH were observed in pgr1, but not in wild-type, suggesting that in wild-type plants signals depending on thylakoid acidification overlay a predominant redox-signal [5].
 

Biological context of MRFAP1

  • These results provide the molecular basis for the interaction between the MRG domain and PAM14, and reveal insights into the potential biological function of MRG15 in transcription regulation and chromatin remodeling [1].
  • Structural and biochemical data together demonstrate that the PAM14 binding site is consisted of residues Ile160, Leu168, Val169, Trp172, Tyr235, Val268, and Arg269 of MRG15, which form a shallow hydrophobic pocket to interact with the N-terminal 50 residues of PAM14 through primarily hydrophobic interactions [1].
 

Physical interactions of MRFAP1

  • The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14 [1].
 

Analytical, diagnostic and therapeutic context of MRFAP1

References

  1. The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14. Zhang, P., Zhao, J., Wang, B., Du, J., Lu, Y., Chen, J., Ding, J. Protein Sci. (2006) [Pubmed]
  2. PAM14, a novel MRG- and Rb-associated protein, is not required for development and T-cell function in mice. Tominaga, K., Magee, D.M., Matzuk, M.M., Pereira-Smith, O.M. Mol. Cell. Biol. (2004) [Pubmed]
  3. MRG15 activates the B-myb promoter through formation of a nuclear complex with the retinoblastoma protein and the novel protein PAM14. Leung, J.K., Berube, N., Venable, S., Ahmed, S., Timchenko, N., Pereira-Smith, O.M. J. Biol. Chem. (2001) [Pubmed]
  4. Multipurpose MRG domain involved in cell senescence and proliferation exhibits structural homology to a DNA-interacting domain. Bowman, B.R., Moure, C.M., Kirtane, B.M., Welschhans, R.L., Tominaga, K., Pereira-Smith, O.M., Quiocho, F.A. Structure (2006) [Pubmed]
  5. Regulation of gene expression by photosynthetic signals triggered through modified CO2 availability. Wormuth, D., Baier, M., Kandlbinder, A., Scheibe, R., Hartung, W., Dietz, K.J. BMC Plant Biol. (2006) [Pubmed]
 
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