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High‐order oligomers of intrinsically disordered brain proteins BASP1 and GAP‐43 preserve the structural disorder

Forsova, Oksana S. ; Zakharov, Vladislav V.

The FEBS journal, 2016-04, Vol.283 (8), p.1550-1569 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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Título:
High‐order oligomers of intrinsically disordered brain proteins BASP1 and GAP‐43 preserve the structural disorder
Autor: Forsova, Oksana S. ; Zakharov, Vladislav V.
Assuntos: Amino Acid Sequence ; Animals ; Assaying ; Axon guidance ; Brain ; Brain - metabolism ; brain proteins BASP1 and GAP‐43 ; Cattle ; Chromatography ; Circular Dichroism ; circular dichroism; fuzzy complexes ; Coils ; Cross-Linking Reagents - pharmacology ; Crosslinking ; Digestion ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; GAP-43 protein ; GAP-43 Protein - chemistry ; GAP-43 Protein - metabolism ; Gel electrophoresis ; Glutaraldehyde ; intrinsically disordered proteins ; Intrinsically Disordered Proteins - chemistry ; Intrinsically Disordered Proteins - metabolism ; Light effects ; Lipid rafts ; Membrane proteins ; Models, Molecular ; Molecular Sequence Data ; Monomers ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Neurochemistry ; Oligomerization ; Oligomers ; Phosphatidylinositol 4,5-diphosphate ; Phospholipids ; Plasticity ; Presynaptic plasticity ; Protein Conformation ; Protein Multimerization ; protein oligomers ; Proteins ; Proteolysis ; Rafts ; Residues ; Sensitivity ; Signal transduction ; Size exclusion chromatography ; Synaptic plasticity
É parte de: The FEBS journal, 2016-04, Vol.283 (8), p.1550-1569
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: Brain acid‐soluble protein‐1 (BASP1) and growth‐associated protein‐43 (GAP‐43) are presynaptic membrane proteins participating in axon guidance, neuroregeneration and synaptic plasticity. They are presumed to sequester phosphatidylinositol‐4,5‐bisphosphate (PIP2) in lipid rafts. Previously we have shown that the proteins form heterogeneously sized oligomers in the presence of anionic phospholipids or SDS at submicellar concentration. BASP1 and GAP‐43 are intrinsically disordered proteins (IDPs). In light of this, we investigated the structure of their oligomers. Using partial cross‐linking of the oligomers with glutaraldehyde, the aggregation numbers of BASP1 and GAP‐43 were estimated as 10–14 and 6–7 monomer subunits, respectively. The cross‐linking pattern indicated that the subunits are circularly arranged. The circular dichroism (CD) spectra of the monomers were characteristic of coil‐like IDPs showing unordered structure with a high population of polyproline‐II conformation. The oligomerization was accompanied by a minor CD spectral change attributable to formation of a small amount of α‐helix. The number of residues in the α‐helical conformation was estimated as 13 in BASP1 and 18 in GAP‐43. However, the overall structure of the oligomers remained disordered, indicating a high degree of ‘fuzziness’. This was confirmed by measuring the hydrodynamic dimensions of the oligomers using polyacrylamide gradient gel electrophoresis and size‐exclusion chromatography, and by assaying their sensitivity to proteolytic digestion. There is evidence that the observed α‐helical folding occurs within the basic effector domains, which are presumably tethered together via anionic molecules of SDS or PIP2. We conclude that BASP1 and GAP‐43 oligomers preserve a mostly disordered structure, which may be of great importance for their function in PIP2 signaling pathway. BASP1 and GAP‐43 are presynaptic membrane proteins which are intrinsically disordered. They form regular oligomers in the presence of anionic phospholipids or SDS. The overall structure of the oligomers proved to be disordered as in ‘fuzzy complexes’. The oligomerization is accompanied by a minor folding attributable to formation of a small amount of α‐helix, probably within the basic effector domains.
Editor: England: Blackwell Publishing Ltd
Idioma: Inglês

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High‐order oligomers of intrinsically disordered brain proteins BASP1 and GAP‐43 preserve the structural disorder

Forsova, Oksana S. ; Zakharov, Vladislav V.

England: Blackwell Publishing Ltd

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