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  • Title: Ca-dependent binding of actin to gelsolin.
    Author: Khaitlina S, Hinssen H.
    Journal: FEBS Lett; 2002 Jun 19; 521(1-3):14-8. PubMed ID: 12067717.
    Abstract:
    Ca(2+) of 0.3-1.0 microM induces both the exposure of tryptic cleavage sites within the gelsolin molecule inaccessible in the Ca-free conformation, and binding of one actin monomer to the N-terminal half of gelsolin. On the other hand, gelsolin-induced enhancement of pyrene actin fluorescence was observed only above 50 microM Ca(2+), and a ternary actin/gelsolin complex preformed in 200 microM Ca(2+) was stable only above 30 microM Ca(2+). These results provide direct evidence for Ca-induced transitions from closed to open conformation of the gelsolin molecule in the range of 3 x 10(-7) to 10(-6) M Ca(2+). They also suggest that Ca(2+)>10(-5) M is required to stabilize actin-actin contacts in the 2:1 actin/gelsolin complex.
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