Actin Capping Protein
نویسندگان
چکیده
منابع مشابه
Mammalian CARMIL inhibits actin filament capping by capping protein.
Actin polymerization in cells occurs via filament elongation at the barbed end. Proteins that cap the barbed end terminate this elongation. Heterodimeric capping protein (CP) is an abundant and ubiquitous protein that caps the barbed end. We find that the mouse homolog of the adaptor protein CARMIL (mCARMIL) binds CP with high affinity and decreases its affinity for the barbed end. Addition of ...
متن کاملCapping protein binding to actin in yeast
The mechanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and the physiological significance of CP binding to actin is not defined. The CP crystal structure suggests that the COOH-terminal regions of the CP alpha and beta subunits bind to the barbed end. Using purified recombinant mutant yeast CP, we tested this model. CP lacking both COOH-terminal regi...
متن کاملEffect of capping protein on the kinetics of actin polymerization.
Acanthamoeba capping protein increased the rate of actin polymerization from monomers with and without calcium. In the absence of calcium, capping protein also increased the critical concentration for polymerization. Various models were evaluated for their ability to predict the effect of capping protein on kinetic curves for actin polymerization under conditions where the critical concentratio...
متن کاملCdc42-induced actin filaments are protected from capping protein
Each actin filament has a pointed and a barbed end, however, filament elongation occurs primarily at the barbed end. Capping proteins, by binding to the barbed end, can terminate this elongation. The rate of capping depends on the concentration of capping protein [1], and thus, if capping terminates elongation, the length of filaments should vary inversely with the concentration of capping prot...
متن کاملActin-capping protein lets epithelial cells take the pressure
Shelterin protein keeps telomeres on edge A member of the shelterin complex helps moor telomeres at the nuclear periphery in worms, Ferreira et al. reveal. Telomeres protect the ends of chromosomes, and the shelterin complex protects telomeres, preventing them from triggering the DNA damage response. Yeast cells shove their telomeres to the fringe of the nucleus, and the marginalized structures...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Circulation Research
سال: 2002
ISSN: 0009-7330,1524-4571
DOI: 10.1161/01.res.0000024389.03152.22