The Role of the FH1 Domain and Profilin in Formin-Mediated Actin-Filament Elongation and Nucleation

• Published in: Current biology Vol. 18; no. 1; pp. 9 - 19
• Main Authors: Paul, Aditya, Pollard, Thomas
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 08.01.2008
• Subjects: Actin Cytoskeleton - metabolism; Amino Acid Sequence; CELLBIO; Microfilament Proteins - chemistry; Microfilament Proteins - metabolism; Microfilament Proteins - physiology; Models, Biological; Molecular Sequence Data; Peptides - chemistry; Peptides - physiology; Profilins - chemistry; Profilins - metabolism; Profilins - physiology; Protein Structure, Tertiary; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae - ultrastructure; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Saccharomyces cerevisiae Proteins - physiology; CELLBIO

Formin proteins nucleate actin filaments de novo and stay associated with the growing barbed end. Whereas the formin-homology (FH) 2 domains mediate processive association, the FH1 domains—in concert with the actin-monomer-binding protein profilin—increase the rate of barbed-end elongation. The mech...