Mammalian CARMIL Inhibits Actin Filament Capping by Capping Protein
Copyright policy )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 mCARMIL to cell extracts increases the rate and extent of Arp2/3 or spectrin-actin seed-induced polymerization. In cells, GFP-mCARMIL concentrates in lamellipodia and increases the fraction of cells with large lamellipodia. Decreasing mCARMIL levels by siRNA transfection lowers the F-actin level and slows cell migration through a mechanism that includes decreased lamellipodia protrusion. This phenotype is reversed by full-length mCARMIL but not mCARMIL lacking the domain that binds CP. Thus, mCARMIL is a key regulator of CP and has profound effects on cell behavior.
- University of Pennsylvania United States
- University of Edinburgh United Kingdom
- University of Mary United States
- Lankenau Institute for Medical Research United States
- Washington University in St. Louis United States
Cell Extracts, Microfilament Proteins, Molecular Sequence Data, In Vitro Techniques, Actins, Protein Structure, Tertiary, Actin Cytoskeleton, Mice, Destrin, Actin Depolymerizing Factors, Cell Movement, Cell Line, Tumor, Mutation, Animals, Humans, Amino Acid Sequence, Pseudopodia, Carrier Proteins, Glioblastoma, Developmental Biology, Protein Binding
Cell Extracts, Microfilament Proteins, Molecular Sequence Data, In Vitro Techniques, Actins, Protein Structure, Tertiary, Actin Cytoskeleton, Mice, Destrin, Actin Depolymerizing Factors, Cell Movement, Cell Line, Tumor, Mutation, Animals, Humans, Amino Acid Sequence, Pseudopodia, Carrier Proteins, Glioblastoma, Developmental Biology, Protein Binding
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