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 journalArticle

5 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 languageEnglish
Pages (from-to)2288-2293
Number of pages6
JournalFEBS Letters
Volume588
Issue number14
DOIs
Publication statusPublished - 27 Jun 2014
Externally publishedYes

Keywords

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

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