Calcium-induced conformational changes in the amino-terminal half of gelsolin |
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Authors: | Roustan Claude Ferjani Imen Maciver Sutherland K Fattoum Abdellatif Rebière Bertrand Benyamin Yves |
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Institution: | UMR 5539 (CNRS) Laboratoire de motilité cellulaire (Ecole Pratique des Hautes Etudes), Université de Montpellier 2, Place E. Bataillon, CC107, 34095 Montpellier Cedex 5, France. |
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Abstract: | Gelsolin is an actin-binding protein that is regulated by the occupancy of multiple calcium-binding sites. We have studied calcium induced conformational changes in the G1-2 and G1-3 sub-domains, and report the binding affinities for the three type II sites. A new probe for G3 has been produced and a K(d) of 5 microM has been measured for calcium in the context of G1-3. The two halves of gelsolin, G1-3 and G4-6 bind weakly with or without calcium, suggesting that once separated by apoptotic proteolysis, G1-3 and G4-6 remain apart allowing G1-3 to sever actin in a calcium free manner. |
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Keywords: | G1-6 the six repeated domains that comprise gelsolin FITC fluoroscein 5-isothiocyanate |
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