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Gene Review

marcks  -  myristoylated alanine rich protein kinase...

Xenopus laevis

 
 
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High impact information on marcks

  • Mutations in the promoter that abolished binding of these two factors also completely inhibited transcriptional activation of the MARCKS gene at MBT [1].
  • By transiently transfecting XTC-2 cells and microinjecting Xenopus embryos with reporter gene constructs containing serial deletions of 5'-flanking MARCKS sequences, we identified a 124-base pair minimal promoter that was critical for promoter activity [1].
  • The binding sites for these two factors are highly conserved in the human and mouse MARCKS promoters, suggesting that these elements might also regulate MARCKS transcription in other species [1].
  • These studies not only increase our knowledge of the transcriptional regulation of the MARCKS genes but also have implications for the mechanisms responsible for zygotic activation of the Xenopus genome at MBT [1].
  • Mechanisms of MARCKS gene activation during Xenopus development [1].
 

Biological context of marcks

  • This study evaluated the transcriptional control of MARCKS gene expression during early development of Xenopus laevis [1].
  • These results are consistent with the notions that phosphorylation of MARCKS reduces its binding affinity for CaM and that the CaM binding affinity of the peptides is coupled to the Ca2+ affinity of CaM [2].
 

Associations of marcks with chemical compounds

  • The myristoylated alanine-rich C kinase substrate (MARCKS) and the MARCKS-related protein (MRP) are members of a distinct family of protein kinase C(PKC) substrates that bind calmodulin (CaM) in a manner regulated by Ca2+ and phosphorylation by PKC [2].
 

Analytical, diagnostic and therapeutic context of marcks

  • We have studies Ca2+ binding of CaM complexed with CaM binding peptides from MARCKS and MRP using flow dialysis, NMR and circular dichroism (CD) spectroscopy [2].

References

  1. Mechanisms of MARCKS gene activation during Xenopus development. Shi, Y., Sullivan, S.K., Pitterle, D.M., Kennington, E.A., Graff, J.M., Blackshear, P.J. J. Biol. Chem. (1997) [Pubmed]
  2. Calcium binding and conformational properties of calmodulin complexed with peptides derived from myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP). Porumb, T., Crivici, A., Blackshear, P.J., Ikura, M. Eur. Biophys. J. (1997) [Pubmed]
 
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