Effects of phosphorylation of the neurofilament L protein on filamentous structures.
AUTOR(ES)
Hisanaga, S
RESUMO
Effects of phosphorylation of the neurofilament L protein (NF-L) on the reassembly system were studied by both sedimentation experiments and low-angle rotary shadowing. Bovine spinal cord NF-L was phosphorylated with 3-4 mol/mol protein by either the catalytic subunit of cAMP-dependent protein kinase or protein kinase C. Phosphorylated NF-L could not assemble into filaments. Phosphorylation by either cAMP-dependent protein kinase or protein kinase C inhibited the same step of the reassembly process. Phosphorylated NF-L remained as an 8-chain complex even in favorable conditions for reassembly. The extent of the effect of phosphorylation on the filamentous structure of NF-L was also investigated by using the catalytic subunit of cAMP-dependent protein kinase. The amount of unassembled NF-L increased linearly with increased phosphorylation in the sedimentation experiments. Structural observations indicated that 1 or 2 mol of phosphorylation is enough to inhibit reassembly and to induce disassembly, and the disassembly process was also observed. The filaments were shown to unravel with disassembly. Star-like clusters, which we reported as being the initial stage of reassembly, were also identified.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=361451Documentos Relacionados
- Isolation and characterization of Candida albicans morphological mutants derepressed for the formation of filamentous hypha-type structures.
- Geometry of interplanar residue contacts in protein structures.
- Protein dynamics derived from clusters of crystal structures.
- Poly(L-alanine) as a universal reference material for understanding protein energies and structures.
- Evaluation of methods for the prediction of membrane protein secondary structures.