title: The effect of intact talin and talin tail fragment on actin filament dynamics and structure depends on pH and ionic strength.
abstract: We employed quasi-elastic light scattering and electron microscopy to investigate the influence of intact talin and talin tail fragment on actin filament dynamics and network structure. Using these methods, we confirm previous reports that intact talin induces cross-linking as well as filament shortening on actin networks. We now show that the effect of intact talin as well as talin tail fragment on actin networks is controlled by pH and ionic strength. At pH 7.5, actin filament dynamics in the presence of intact talin and talin tail fragment are characterized by a rapid decay of the dynamic structure factor and by a square root power law for the stretched exponential decay which is in contrast with the theory for pure actin solutions. At pH 6 and low ionic strength, intact talin cross-links actin filaments more tightly than talin tail fragment. Talin head fragment showed no effect on actin networks, indicating that the actin binding sites reside probably exclusively within the tail domain.
authors: Department of Pathology, Children's Hospital, Harvard Medical School, Boston, USA. GOLDMANN_W@a1.tch.harvard.edu
authors: W H
authors: WH
authors: Goldmann
authors: D
authors: D
authors: Hess
authors: G
authors: G
authors: Isenberg
mesh_terms: D000199:Actins / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D006863:Hydrogen-Ion Concentration; D008027:Light; D008854:Microscopy, Electron; D009994:Osmolar Concentration; D010446:Peptide Fragments / Q000494:pharmacology*; D011817:Rabbits; D012542:Scattering, Radiation; D013329:Structure-Activity Relationship; D016608:Talin / Q000494:pharmacology*
chemical_list: D000199:Actins; D010446:Peptide Fragments; D016608:Talin