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Dimerization of profilin II upon binding the (GP 5 ) 3 peptide from VASP overcomes the inhibition of actin nucleation by profilin II and thymosin β4
Author(s) -
Jonckheere Veronique,
Lambrechts Anja,
Vandekerckhove Joël,
Ampe Christophe
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00293-8
Subject(s) - profilin , peptide , actin , chemistry , actin binding protein , protein filament , mdia1 , actina , biophysics , actin remodeling , biochemistry , biology , actin cytoskeleton , cytoskeleton , cell
Profilin II dimers bind the (GP 5 ) 3 peptide derived from VASP with an affinity of approximately 0.5 μM. The resulting profilin II‐peptide complex overcomes the combined capacity of thymosin β4 and profilin II to inhibit actin nucleation and restores the extent of filament formation. We do not observe such an effect when barbed filament ends are capped. Neither can profilin I, in the presence of the peptide, promote actin polymerization during its early phase consistent with a lower affinity. Since a Pro 17 peptide‐profilin II complex only partially restores actin polymerization, the glycine residues in the VASP peptide appear important.