Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin.

This publication has 52 references indexed in Scilit:

• Microinjection of gelsolin into living cells.
  The Journal of cell biology, 1987
• Kinetics of actin monomer exchange at the slow growing ends of actin filaments and their relation to the elongation of filaments shortened by gelsolin
  Journal of Muscle Research and Cell Motility, 1986
• Phorbol ester induces rapid actin assembly in neutrophil leucocytes independently of changes in [Ca2+]i and pHi
  Journal of Muscle Research and Cell Motility, 1986
• Common domain structure of Ca²⁺ and lipid‐binding proteins
  FEBS Letters, 1986
• Sequential binding of actin monomers to plasma gelsolin and its inhibition by vitamin D-binding protein
  Biochemical and Biophysical Research Communications, 1986
• Bovine serum brevin
  European Journal of Biochemistry, 1985
• The effect of plasma gelsolin on actin filaments Ca2+-dependency of the capping and severing activities
  Biochemical and Biophysical Research Communications, 1985
• Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking
  Biochemistry, 1985
• A 90 000-dalton actin-binding protein from platelets comparison with villin and plasma brevin
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976