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PMID:9017597

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Citation

Prassler, J, Stocker, S, Marriott, G, Heidecker, M, Kellermann, J and Gerisch, G (1997) Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes. Mol. Biol. Cell 8:83-95

Abstract

A protein purified from cytoskeletal fractions of Dictyostelium discoideum proved to be a member of the fimbrin/plastin family of actin-bundling proteins. Like other family members, this Ca(2+)-inhibited 67-kDa protein contains two EF hands followed by two actin-binding sites of the alpha-actinin/beta-spectrin type. Dd plastin interacted selectively with actin isoforms: it bound to D. discoideum actin and to beta/gamma-actin from bovine spleen but not to alpha-actin from rabbit skeletal muscle. Immunofluorescence labeling of growth phase cells showed accumulation of Dd plastin in cortical structures associated with cell surface extensions. In the elongated, streaming cells of the early aggregation stage, Dd plastin was enriched in the front regions. To examine how the bundled actin filaments behave in myosin II-driven motility, complexes of F-actin and Dd plastin were bound to immobilized heavy meromyosin, and motility was started by photoactivating caged ATP. Actin filaments were immediately propelled out of bundles or even larger aggregates and moved on the myosin as separate filaments. This result shows that myosin can disperse an actin network when it acts as a motor and sheds light on the dynamics of protein-protein interactions in the cortex of a motile cell where myosin II and Dd plastin are simultaneously present.

Links

PubMed PMC276061

Keywords

Actins/metabolism; Actins/ultrastructure; Amino Acid Sequence; Animals; Binding Sites; Calcium/metabolism; Calcium/pharmacology; Cattle; Cross-Linking Reagents; Dictyostelium/chemistry; Dictyostelium/growth & development; Dictyostelium/ultrastructure; Membrane Glycoproteins/chemistry; Membrane Glycoproteins/metabolism; Microfilament Proteins; Molecular Sequence Data; Muscle, Skeletal/chemistry; Myosins/metabolism; Myosins/ultrastructure; Phosphoproteins/chemistry; Phosphoproteins/genetics; Phosphoproteins/metabolism; Rabbits; Sequence Homology, Amino Acid; Spleen/chemistry

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

DICDI:FIMB

enables

GO:0005509: calcium ion binding

ECO:0000250: sequence similarity evidence used in manual assertion

F

Seeded From UniProt

complete

DICDI:FIMB

located_in

GO:0030027: lamellipodium

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DICDI:FIMB

located_in

GO:0031252: cell leading edge

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DICDI:FIMB

involved_in

GO:0051017: actin filament bundle assembly

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

DICDI:FIMB

enables

GO:0051015: actin filament binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

See also

References

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