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• W2287127968 endingPage "1569" @default.
• W2287127968 startingPage "1550" @default.
• W2287127968 abstract "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." @default.
• W2287127968 created "2016-06-24" @default.
• W2287127968 creator A5040753627 @default.
• W2287127968 creator A5041459897 @default.
• W2287127968 date "2016-03-11" @default.
• W2287127968 modified "2023-09-23" @default.
• W2287127968 title "High-order oligomers of intrinsically disordered brain proteins BASP1 and GAP-43 preserve the structural disorder" @default.
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• W2287127968 doi "https://doi.org/10.1111/febs.13692" @default.
• W2287127968 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26918762" @default.

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