PMID- 25207437 OWN - NLM STAT- MEDLINE DCOM- 20141118 LR - 20211021 IS - 1471-0080 (Electronic) IS - 1471-0072 (Print) IS - 1471-0072 (Linking) VI - 15 IP - 10 DP - 2014 Oct TI - Capping protein regulators fine-tune actin assembly dynamics. PG - 677-89 LID - 10.1038/nrm3869 [doi] AB - Capping protein (CP) binds the fast growing barbed end of the actin filament and regulates actin assembly by blocking the addition and loss of actin subunits. Recent studies provide new insights into how CP and barbed-end capping are regulated. Filament elongation factors, such as formins and ENA/VASP (enabled/vasodilator-stimulated phosphoprotein), indirectly regulate CP by competing with CP for binding to the barbed end, whereas other molecules, including V-1 and phospholipids, directly bind to CP and sterically block its interaction with the filament. In addition, a diverse and unrelated group of proteins interact with CP through a conserved 'capping protein interaction' (CPI) motif. These proteins, including CARMIL (capping protein, ARP2/3 and myosin I linker), CD2AP (CD2-associated protein) and the WASH (WASP and SCAR homologue) complex subunit FAM21, recruit CP to specific subcellular locations and modulate its actin-capping activity via allosteric effects. FAU - Edwards, Marc AU - Edwards M AD - Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110, USA. FAU - Zwolak, Adam AU - Zwolak A AD - Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. FAU - Schafer, Dorothy A AU - Schafer DA AD - Departments of Biology and Cell Biology, University of Virginia, Charlottesville, Virginia 22904, USA. FAU - Sept, David AU - Sept D AD - Department of Biomedical Engineering and Center for Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan 48109, USA. FAU - Dominguez, Roberto AU - Dominguez R AD - Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. FAU - Cooper, John A AU - Cooper JA AD - Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110, USA. LA - eng GR - R01 GM038542/GM/NIGMS NIH HHS/United States GR - MH087950/MH/NIMH NIH HHS/United States GR - GM038542/GM/NIGMS NIH HHS/United States GR - 5T90DA02287104/DA/NIDA NIH HHS/United States GR - R01 MH087950/MH/NIMH NIH HHS/United States GR - GM073791/GM/NIGMS NIH HHS/United States GR - R01 GM095509/GM/NIGMS NIH HHS/United States GR - GM095509/GM/NIGMS NIH HHS/United States GR - R01 GM073791/GM/NIGMS NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Review DEP - 20140910 PL - England TA - Nat Rev Mol Cell Biol JT - Nature reviews. Molecular cell biology JID - 100962782 RN - 0 (Actin Capping Proteins) RN - 0 (Adaptor Proteins, Signal Transducing) RN - 0 (CARMIL1 protein, human) RN - 0 (CD2-associated protein) RN - 0 (Carrier Proteins) RN - 0 (Cytoskeletal Proteins) RN - 0 (DNA-Binding Proteins) RN - 0 (ENA-VASP proteins) RN - 0 (Microfilament Proteins) RN - 0 (Phosphatidylinositol Phosphates) RN - 0 (WASH protein, human) SB - IM EIN - Nat Rev Mol Cell Biol. 2014 Nov;15(11):701 MH - Actin Capping Proteins/*metabolism/physiology MH - Actin Cytoskeleton/*physiology MH - Adaptor Proteins, Signal Transducing/metabolism/physiology MH - Amino Acid Sequence MH - Carrier Proteins/metabolism/physiology MH - Cytoskeletal Proteins/metabolism/physiology MH - DNA-Binding Proteins/*metabolism/physiology MH - Humans MH - Microfilament Proteins/metabolism/physiology MH - Models, Molecular MH - Phosphatidylinositol Phosphates/chemistry MH - Protein Binding MH - Protein Conformation PMC - PMC4271544 MID - NIHMS647391 EDAT- 2014/09/11 06:00 MHDA- 2014/11/19 06:00 PMCR- 2014/12/19 CRDT- 2014/09/11 06:00 PHST- 2014/09/11 06:00 [entrez] PHST- 2014/09/11 06:00 [pubmed] PHST- 2014/11/19 06:00 [medline] PHST- 2014/12/19 00:00 [pmc-release] AID - nrm3869 [pii] AID - 10.1038/nrm3869 [doi] PST - ppublish SO - Nat Rev Mol Cell Biol. 2014 Oct;15(10):677-89. doi: 10.1038/nrm3869. Epub 2014 Sep 10.