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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Authors: | Chen Zhao Chengcheng Liu Christopher W.V. Hogue Boon Chuan Low |
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Affiliation: | 1. Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore;2. Bioprocessing Technology Institute, Agency for Science, Technology and Research, Singapore 138668, Singapore;3. Mechanobiology Institute, National University of Singapore, Singapore 117411, Singapore |
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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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Keywords: | Filopodium Actin filament Formin Disordered Conformational change &ldquo jack&rdquo Model |
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