Microtubule-associated protein interactions with actin filaments: evidence for differential behavior of neuronal MAP-2 and tau in the presence of phosphatidyl-inositol.
Microtubule-associated protein (MAP) interactions with actin were investigated by falling-ball viscometry. At 1-2 microM MAP-2 or tau, we obtained a critical gelation concentration for actin of 0.1 mg/ml. In the presence of phosphatidyl-inositol, actin filament bundling was completely disrupted only when MAP-2 served as the cross-linker, whereas tau-induced bundling of actin was unaffected by phosphatidyl-inositol. This represents the first clear indication that MAP-2 and tau exhibit differential behavior in their interaction with cytoskeletal components.
Yamauchi
P S
PS
Department of Biochemistry and Molecular Biology University of Florida College of Medicine, Gainesville 32610-0245.
Purich
D L
DL
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D066298:In Vitro Techniques; D008840:Microfilament Proteins / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010716:Phosphatidylinositols / Q000494:pharmacology*; D011485:Protein Binding; D011817:Rabbits; D014783:Viscosity; D016875:tau Proteins / Q000378:metabolism*
D000199:Actins; D008840:Microfilament Proteins; D008869:Microtubule-Associated Proteins; D009419:Nerve Tissue Proteins; D010716:Phosphatidylinositols; D016875:tau Proteins