Interaction of myelin basic protein and proteolipid protein

@article{Edwards1989InteractionOM,
  title={Interaction of myelin basic protein and proteolipid protein},
  author={Anthony M. Edwards and N W Ross and Jeffrey B. Ulmer and Peter E. Braun},
  journal={Journal of Neuroscience Research},
  year={1989},
  volume={22}
}
The interaction of myelin basic protein (MBP) and proteolipid protein (PLP) was studied using a microtitre well binding assay and the ligand‐blot overlay technique. The binding of iodinated PLP to MBP that was immobilized on microtitre wells was saturable and reversible. Its selectivity was investigated by the ligand‐blot overlay technique. Iodinated PLP was found to bind MBP but not any other CNS myelin proteins. This interaction was not dependent on the phosphoryl moiety of MBP. Binding of… 
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The structural characteristics of myelin basic protein (MBP) involved in protein‐protein and protein‐lipid interactions were investigated and suggest that MBP may contain a hydrophobic domain similar to those in the other well‐characterized CaM‐binding proteins.
Identification of GTP‐ binding proteins in myelin and oligodendrocyte membranes
TLDR
None of the well‐known myelin proteins bound GTP by the procedure described, and the total membrane fraction of cultured oligodendrocytes is associated with both groups of GTP‐binding proteins.
Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoylphosphatidylglycerol.
TLDR
Quantitation of protein and lipid contents in the MBP-PLP-DMPG double recombinants at different PLP:DMPG ratios led to the conclusion that MBP binds only to the DMPG lipid headgroups and is hindered from interaction with the first shell of lipids surrounding the PLP.
A Tale of Two Citrullines—Structural and Functional Aspects of Myelin Basic Protein Deimination in Health and Disease
TLDR
The degree of deimination (or citrullination) of MBP is correlated with the severity of MS, and may represent a primary defect that precedes neurodegeneration due to autoimmune attack, which indicates that this modification plays major physiological roles in myelin assembly.
Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis.
The Basic Protein of CNS Myelin: Its Structure and Ligand Binding
  • R. Smith
  • Biology, Chemistry
    Journal of neurochemistry
  • 1992
TLDR
Current evidence suggests that the protein has a structural role within myelin and that its own three-dimensional structure is strongly dependent on the molecules with which it is associated, and studies of the isolated protein or of the protein in reconstituted lipid systems may yield, at best, a rough guide to the structure within its biological environment.
Three-dimensional Structure of Myelin Basic Protein
TLDR
These results are the first structures achieved directly for this unusual macromolecule, which plays a key role in the development of multiple sclerosis.
Myelin proteolipid protein, basic protein, the small isoform of myelin‐associated glycoprotein, and p42MAPK are associated in the Triton X‐100 extract of central nervous system myelin
TLDR
Lipid analysis revealed that the PLP–MBP–S‐MAG coimmunoprecipitated with some phospholipids and sulfatide but not cholesterol or galactosylceramide, indicating that the lipid/protein ratio is low, and the complex had a high density.
Myelin basic protein component C1 in increasing concentrations can elicit fusion, aggregation, and fragmentation of myelin-like membranes.
TLDR
The results showed that the phenomena of vesicle fusion, aggregation, and fragmentation can all be observed in one in vitro system, but were dependent on lipid composition and on the relative proportions of protein and lipid.
Proteolipid protein interactions in transfectants: Implications for myelin assembly
TLDR
Since, in HeLa cells at least, the delivery of PLP to the plasma membrane is facilitated by the coexpression of DM20, it is suggested that the two proteins interact intracellularly to form a complex.
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References

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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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