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Gene Review

MARCKS  -  myristoylated alanine-rich protein kinase...

Gallus gallus

 
 
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High impact information on LOC396473

 

Biological context of LOC396473

  • Identification of the chicken MARCKS phosphorylation site specific for differentiating neurons as Ser 25 using a monoclonal antibody and mass spectrometry [4].
  • Here we show that the most outstanding modifications occur at the outer retina, where S25p disappears at the end of embryonic development and where MARCKS is missing in adults [5].
  • Myristoylated alanine-rich kinase C substrate (MARCKS), an actin-binding protein, is involved in several signal transduction pathways [5].
  • Analysis of differential gene expression supports a role for amyloid precursor protein and a protein kinase C substrate (MARCKS) in long-term memory [6].
 

Anatomical context of LOC396473

  • These results also suggest that PKC-theta-controlled MARCKS translocation is associated with, or a requisite event for, myoblast fusion [3].
  • Immunostaining of the cultured myoblasts also revealed that MARCKS translocated from the cytosol to the plasma membrane and to the peripheral region of nuclei as the mononucleated myoblasts fused to form multinucleated myotubes [3].
  • Intact ciliary ganglia remained viable for several hours after dissection and, after incubation with 32P(i), responded to phorbol ester stimulation by an increased endogenous phosphorylation of several proteins, but especially myristoylated alanine-rich C kinase substrate [7].
  • We previously described the purification of MARCKS from chick embryo brain, using a monoclonal antibody (mAb 3C3), raised against embryonic neural retina [8].
  • We used it to explore the appearance and developmental progression of phospho-MARCKS (ph-MARCKS) during initial stages of neurogenesis in retina and spinal cord, and compared its distribution with total MARCKS [8].
 

Associations of LOC396473 with chemical compounds

  • MARCKS is an actin-modulating protein that can be phosphorylated in multiple sites by PKC and proline-directed kinases [4].
  • The phosphorylation of the myristoylated alanine-rich protein kinase C substrate (MARCKS) in the left intermediate and medial hyperstriatum ventrale (IMHV) of the chick brain has been shown previously to correlate significantly with the strength of learning in filial imprinting [9].
 

Analytical, diagnostic and therapeutic context of LOC396473

References

  1. Learning selectively increases protein kinase C substrate phosphorylation in specific regions of the chick brain. Sheu, F.S., McCabe, B.J., Horn, G., Routtenberg, A. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  2. Molecular cloning, sequence, and expression of a cDNA encoding the chicken myristoylated alanine-rich C kinase substrate (MARCKS). Graff, J.M., Stumpo, D.J., Blackshear, P.J. Mol. Endocrinol. (1989) [Pubmed]
  3. Involvement of the theta-type protein kinase C in translocation of myristoylated alanine-rich C kinase substrate (MARCKS) during myogenesis of chick embryonic myoblasts. Kim, S.S., Kim, J.H., Kim, H.S., Park, D.E., Chung, C.H. Biochem. J. (2000) [Pubmed]
  4. Identification of the chicken MARCKS phosphorylation site specific for differentiating neurons as Ser 25 using a monoclonal antibody and mass spectrometry. Zolessi, F.R., Durán, R., Engström, U., Cerveñansky, C., Hellman, U., Arruti, C. J. Proteome Res. (2004) [Pubmed]
  5. MARCKS in advanced stages of neural retina histogenesis. Zolessi, F.R., Arruti, C. Dev. Neurosci. (2004) [Pubmed]
  6. Analysis of differential gene expression supports a role for amyloid precursor protein and a protein kinase C substrate (MARCKS) in long-term memory. Solomonia, R.O., Morgan, K., Kotorashvili, A., McCabe, B.J., Jackson, A.P., Horn, G. Eur. J. Neurosci. (2003) [Pubmed]
  7. Characterization of protein kinase and phosphatase systems in chick ciliary ganglion. Lengyel, I., Nichol, K.A., Sim, A.T., Bennett, M.R., Dunkley, P.R., Rostas, J.A. Neuroscience (1996) [Pubmed]
  8. Sustained phosphorylation of MARCKS in differentiating neurogenic regions during chick embryo development. Zolessi, F.R., Arruti, C. Brain Res. Dev. Brain Res. (2001) [Pubmed]
  9. Differential distribution of protein kinase C (PKC alpha beta and PKC gamma) isoenzyme immunoreactivity in the chick brain. Van der Zee, E.A., Bolhuis, J.J., Solomonia, R.O., Horn, G., Luiten, P.G. Brain Res. (1995) [Pubmed]
 
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