A Cooperative jack model of random coil-to-elongation transition of the FH1 domain by profilin binding explains formin motor behavior in actin polymerization

Chen Zhao; Chengcheng Liu; Christopher W. V. Hogue; Boon Chuan Low

doi:10.1016/j.febslet.2014.05.016

A Cooperative jack model of random coil-to-elongation transition of the FH1 domain by profilin binding explains formin motor behavior in actin polymerization

Chen Zhao, Chengcheng Liu, Christopher W. V. Hogue, Boon Chuan Low

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

7 Citations (Scopus)

Abstract

Filopodia are essential for the development of neuronal growth cones, cell polarity and cell migration. Their protrusions are powered by the polymerization of actin filaments linked to the plasma membrane, catalyzed by formin proteins. The acceleration of polymerization depends on the number of profilin-actins binding with the formin-FH1 domain. Biophysical characterization of the disordered formin-FH1 domain remains a challenge. We analyzed the conformational distribution of the diaphanous-related formin mDia1-FH1 bound with one to six profilins. We found a coil-to-elongation transition in the FH1 domain. We propose a cooperative "jack" model for the Formin-Homology-1 (FH1) domain of formins stacked by profilin-actins.

Original language	English
Pages (from-to)	2288-2293
Number of pages	6
Journal	FEBS Letters
Volume	588
Issue number	14
DOIs	https://doi.org/10.1016/j.febslet.2014.05.016
Publication status	Published - 27 Jun 2014
Externally published	Yes

Keywords

Filopodium
Actin filament
Formin
Disordered
Conformational change
“Jack” Model
"jack" Model

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10.1016/j.febslet.2014.05.016

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abstract = "Filopodia are essential for the development of neuronal growth cones, cell polarity and cell migration. Their protrusions are powered by the polymerization of actin filaments linked to the plasma membrane, catalyzed by formin proteins. The acceleration of polymerization depends on the number of profilin-actins binding with the formin-FH1 domain. Biophysical characterization of the disordered formin-FH1 domain remains a challenge. We analyzed the conformational distribution of the diaphanous-related formin mDia1-FH1 bound with one to six profilins. We found a coil-to-elongation transition in the FH1 domain. We propose a cooperative {"}jack{"} model for the Formin-Homology-1 (FH1) domain of formins stacked by profilin-actins.",

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AU - Zhao, Chen

AU - Liu, Chengcheng

AU - Hogue, Christopher W. V.

AU - Low, Boon Chuan

PY - 2014/6/27

Y1 - 2014/6/27

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AB - Filopodia are essential for the development of neuronal growth cones, cell polarity and cell migration. Their protrusions are powered by the polymerization of actin filaments linked to the plasma membrane, catalyzed by formin proteins. The acceleration of polymerization depends on the number of profilin-actins binding with the formin-FH1 domain. Biophysical characterization of the disordered formin-FH1 domain remains a challenge. We analyzed the conformational distribution of the diaphanous-related formin mDia1-FH1 bound with one to six profilins. We found a coil-to-elongation transition in the FH1 domain. We propose a cooperative "jack" model for the Formin-Homology-1 (FH1) domain of formins stacked by profilin-actins.

KW - Filopodium

KW - Actin filament

KW - Formin

KW - Disordered

KW - Conformational change

KW - “Jack” Model

KW - "jack" Model

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A Cooperative jack model of random coil-to-elongation transition of the FH1 domain by profilin binding explains formin motor behavior in actin polymerization

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Keywords

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