Localization of a myosin heavy chain-like polypeptide to Drosophila nuclear pore complexes.
AUTOR(ES)
Berrios, M
RESUMO
Antibodies previously used for immunofluorescence localization of a myosin heavy chain-like polypeptide to the nuclear envelope in higher eukaryotic cells crossreact with both muscle and nonmuscle isoforms of Drosophila myosin heavy chain. Analyses of Drosophila tissue culture cells and premyogenic embryos suggest that it is the nonmuscle isoform that is associated with the nuclear envelope. Further immunofluorescence and immunoelectron microscopy indicate that this polypeptide is associated with nuclear pore complexes. These data support the hypothesis put forward previously that myosin or myosin-like molecules play a role in pore complex architecture.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=50781Documentos Relacionados
- Further characterization and in situ localization of chain-like aggregates of the gliding bacteria Myxococcus fulvus and Myxococcus xanthus.
- Import of simian virus 40 virions through nuclear pore complexes.
- The heavy chain of Acanthamoeba myosin IB is a fusion of myosin-like and non-myosin-like sequences.
- Localization of myosin heavy chain A in the human pathogen Entamoeba histolytica.
- Disruption of the nucleoporin gene NUP133 results in clustering of nuclear pore complexes.