Activation in isolation: Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin

Kartik Narayan; Sakesit Chumnarnsilpa; Han Choe; Edward Irobi; Dunja Urosev; Uno Lindberg; Clarence E. Schutt; Leslie D. Burtnick; Robert C. Robinson

doi:10.1016/S0014-5793(03)00933-5

Activation in isolation: Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin

Kartik Narayan, Sakesit Chumnarnsilpa, Han Choe, Edward Irobi, Dunja Urosev, Uno Lindberg, Clarence E. Schutt, Leslie D. Burtnick, Robert C. Robinson

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

26 Citations (Scopus)

Abstract

Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 Å resolution in the presence of Ca²⁺ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca²⁺ sites occupied. Neither actin nor the type-l Ca²⁺, which normally is sandwiched between actin and G4, is required to achieve this conformation.

Original language	English
Pages (from-to)	82-85
Number of pages	4
Journal	FEBS Letters
Volume	552
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(03)00933-5
Publication status	Published - Sept 25 2003
Externally published	Yes

Keywords

Actin
Calcium-activation
Gelsolin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(03)00933-5

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title = "Activation in isolation: Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin",

abstract = "Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 {\AA} resolution in the presence of Ca2+ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca2+ sites occupied. Neither actin nor the type-l Ca2+, which normally is sandwiched between actin and G4, is required to achieve this conformation.",

keywords = "Actin, Calcium-activation, Gelsolin",

author = "Kartik Narayan and Sakesit Chumnarnsilpa and Han Choe and Edward Irobi and Dunja Urosev and Uno Lindberg and Schutt, {Clarence E.} and Burtnick, {Leslie D.} and Robinson, {Robert C.}",

note = "Funding Information: We thank Terese Bergfors for crystalliztion facilities. We acknowledge the ESRF for provision of synchrotron radiation facilities and thank Raimond Ravelli for assistance in using beamline 14-4. For financial support, we thank the Swedish Natural Science Research Council (R.C.R. and U.L.), and the Heart and Stroke Foundation of BC and the Yukon (L.D.B.). K.N. thanks the Swedish Foundation for International Cooperation in Research and Higher Education (STINT) for support through a grant to U.L.",

year = "2003",

month = sep,

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doi = "10.1016/S0014-5793(03)00933-5",

language = "English",

volume = "552",

pages = "82--85",

journal = "FEBS Letters",

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TY - JOUR

T1 - Activation in isolation

T2 - Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin

AU - Narayan, Kartik

AU - Chumnarnsilpa, Sakesit

AU - Choe, Han

AU - Irobi, Edward

AU - Urosev, Dunja

AU - Lindberg, Uno

AU - Schutt, Clarence E.

AU - Burtnick, Leslie D.

AU - Robinson, Robert C.

N1 - Funding Information: We thank Terese Bergfors for crystalliztion facilities. We acknowledge the ESRF for provision of synchrotron radiation facilities and thank Raimond Ravelli for assistance in using beamline 14-4. For financial support, we thank the Swedish Natural Science Research Council (R.C.R. and U.L.), and the Heart and Stroke Foundation of BC and the Yukon (L.D.B.). K.N. thanks the Swedish Foundation for International Cooperation in Research and Higher Education (STINT) for support through a grant to U.L.

PY - 2003/9/25

Y1 - 2003/9/25

N2 - Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 Å resolution in the presence of Ca2+ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca2+ sites occupied. Neither actin nor the type-l Ca2+, which normally is sandwiched between actin and G4, is required to achieve this conformation.

AB - Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 Å resolution in the presence of Ca2+ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca2+ sites occupied. Neither actin nor the type-l Ca2+, which normally is sandwiched between actin and G4, is required to achieve this conformation.

KW - Actin

KW - Calcium-activation

KW - Gelsolin

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DO - 10.1016/S0014-5793(03)00933-5

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AN - SCOPUS:0141537902

SN - 0014-5793

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JF - FEBS Letters

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ER -

Activation in isolation: Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin

Abstract

Keywords

ASJC Scopus subject areas

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