Ca-dependent binding of actin to gelsolin

Khaitlina S, Hinssen H (2002)
FEBS LETTERS 521(1-3): 14-18.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Khaitlina, S; Hinssen, HorstUniBi
Abstract / Bemerkung
Ca2+ of 0.3-1.0 muM 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 muM Ca2+, and a ternary actin/gelsolin complex preformed in 200 muM Ca2+ was stable only above 30 muM Ca2+. These results provide direct evidence for a Ca-induced transitions from closed to open conformation of the gelsolin molecule in the range of 3 x 10(-7) to 10(-6) M Ca2+. They also suggest that Ca2+ > 10(-5) M is required to stabilize actin-actin contacts in the 2:1 actin/gelsolin complex. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
limited proteolysis; Ca-dependence; actin; formation; gelsolin; complex; conformational change
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Khaitlina S, Hinssen H. Ca-dependent binding of actin to gelsolin. FEBS LETTERS. 2002;521(1-3):14-18.
Khaitlina, S., & Hinssen, H. (2002). Ca-dependent binding of actin to gelsolin. FEBS LETTERS, 521(1-3), 14-18.
Khaitlina, S, and Hinssen, Horst. 2002. “Ca-dependent binding of actin to gelsolin”. FEBS LETTERS 521 (1-3): 14-18.
Khaitlina, S., and Hinssen, H. (2002). Ca-dependent binding of actin to gelsolin. FEBS LETTERS 521, 14-18.
Khaitlina, S., & Hinssen, H., 2002. Ca-dependent binding of actin to gelsolin. FEBS LETTERS, 521(1-3), p 14-18.
S. Khaitlina and H. Hinssen, “Ca-dependent binding of actin to gelsolin”, FEBS LETTERS, vol. 521, 2002, pp. 14-18.
Khaitlina, S., Hinssen, H.: Ca-dependent binding of actin to gelsolin. FEBS LETTERS. 521, 14-18 (2002).
Khaitlina, S, and Hinssen, Horst. “Ca-dependent binding of actin to gelsolin”. FEBS LETTERS 521.1-3 (2002): 14-18.

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