Calcium-induced conformational changes in the amino-terminal half of gelsolin

Claude Roustan; Imen Ferjani; Sutherland K. Maciver; Abdellatif Fattoum; Bertrand Rebière; Yves Benyamin

doi:10.1016/j.febslet.2007.01.031

Calcium-induced conformational changes in the amino-terminal half of gelsolin

Claude Roustan^*
, Imen Ferjani
, Sutherland K. Maciver
, Abdellatif Fattoum
, Bertrand Rebière
, Yves Benyamin

^*Corresponding author for this work

School of Neurological and Cardiovascular Sciences

Research output: Contribution to journal › Article › peer-review

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 μM 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.

Original language	English
Pages (from-to)	681-686
Number of pages	6
Journal	FEBS Letters
Volume	581
Issue number	4
Early online date	22 Jan 2007
DOIs	https://doi.org/10.1016/j.febslet.2007.01.031
Publication status	Published - 20 Feb 2007

Keywords / Materials (for Non-textual outputs)

Actin cytoskeleton
Apoptosis
Calcium-binding
Gelsolin

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10.1016/j.febslet.2007.01.031

Cite this

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title = "Calcium-induced conformational changes in the amino-terminal half of gelsolin",

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 Kd of 5 μM 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.",

keywords = "Actin cytoskeleton, Apoptosis, Calcium-binding, Gelsolin",

author = "Claude Roustan and Imen Ferjani and Maciver, \{Sutherland K.\} and Abdellatif Fattoum and Bertrand Rebi{\`e}re and Yves Benyamin",

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T1 - Calcium-induced conformational changes in the amino-terminal half of gelsolin

AU - Roustan, Claude

AU - Ferjani, Imen

AU - Maciver, Sutherland K.

AU - Fattoum, Abdellatif

AU - Rebière, Bertrand

AU - Benyamin, Yves

PY - 2007/2/20

Y1 - 2007/2/20

N2 - 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 Kd of 5 μM 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.

AB - 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 Kd of 5 μM 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.

KW - Actin cytoskeleton

KW - Apoptosis

KW - Calcium-binding

KW - Gelsolin

UR - https://www.scopus.com/pages/publications/33846844868

U2 - 10.1016/j.febslet.2007.01.031

DO - 10.1016/j.febslet.2007.01.031

M3 - Article

C2 - 17258204

AN - SCOPUS:33846844868

SN - 0014-5793

VL - 581

SP - 681

EP - 686

JO - FEBS Letters

JF - FEBS Letters

IS - 4

ER -

Calcium-induced conformational changes in the amino-terminal half of gelsolin

Abstract

Keywords / Materials (for Non-textual outputs)

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