High impact information on corA

• Coronin involved in phagocytosis: dynamics of particle-induced relocalization visualized by a green fluorescent protein Tag [1].
• A fusion of coronin with green fluorescent protein (GFP) accumulates in the cups within less than 1 min upon attachment of a particle and is gradually released from the phagosome within 1 min after engulfment is completed [1].
• These include the cleavage furrow protein cortexillin I, a novel protein we named dynacortin, an ezrin-radixin-moesin-family protein, and coronin [2].
• When these cor- cells grow in liquid medium they become multinucleate, indicating a role of coronin in cytokinesis [3].
• Dictyostelium mutants lacking the cytoskeletal protein coronin are defective in cytokinesis and cell motility [3].

Biological context of corA

• RESULTS: We have visualized the redistribution of coronin by fluorescence imaging of motile cells that have been transfected with an expression plasmid containing the coding sequence of coronin fused to the sequence encoding the green fluorescent protein (GFP) [4].

Anatomical context of corA

• This protein with a relative molecular mass of 55 kDa has been named coronin because of its association with crown-shaped cell surface projections of growth-phase D. discoideum cells [5].
• It is hypothesized that coronin is implicated in the transmission of chemotactic signals from cAMP receptors in the plasma membrane through G proteins to the cortical cytoskeleton, whose structure and activity is locally modulated [5].
• CONCLUSIONS: These data demonstrate that coronin is reversibly recruited from the cytoplasm and is incorporated into the actin network of a nascent leading edge, where it participates in the reorganization of the cytoskeleton [4].

Associations of corA with chemical compounds

• In aggregating cells, which respond most sensitively to the chemoattractant cyclic AMP, coronin is accumulated at the front where surface projections are directed towards a cAMP source [5].
• First, nascent phagosomes were associated with coronin and rapidly received a lysosomal glycoprotein, LmpB [6].
• T. vaginalis coronin had 50% similarity with the coronin family, possessing the five WD-repeats and a leucine zipper in its C-terminal part [7].

Other interactions of corA

• The coronin mutant and the myoA/B double myosin I mutant were more permissive than wild-type strains for intracellular growth [8].

Analytical, diagnostic and therapeutic context of corA

• To explore this role, coronin has been localized in mitotic wild-type cells by immunofluorescence labeling [3].
• Immunogold electron microscopy confirmed the coronin labeling in the actin-rich microfilamentous fringe beneath the plasma membrane, with accumulation in phagocytic zones and pseudopodial extensions [7].

References