Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The . gov means it’s official. Federal government websites often end in . gov or . mil VSports app下载. Before sharing sensitive information, make sure you’re on a federal government site. .

Https

The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely. V体育官网.

Review
. 2013 Aug 1;126(Pt 15):3249-58.
doi: 10.1242/jcs.128231.

The role of cyclase-associated protein in regulating actin filament dynamics - more than a monomer-sequestration factor

Shoichiro Ono  1
Affiliations
Review

The role of cyclase-associated protein in regulating actin filament dynamics - more than a monomer-sequestration factor

Shoichiro Ono. J Cell Sci. .

Abstract

Dynamic reorganization of the actin cytoskeleton is fundamental to a number of cell biological events. A variety of actin-regulatory proteins modulate polymerization and depolymerization of actin and contribute to actin cytoskeletal reorganization. Cyclase-associated protein (CAP) is a conserved actin-monomer-binding protein that has been studied for over 20 years. Early studies have shown that CAP sequesters actin monomers; recent studies, however, have revealed more active roles of CAP in actin filament dynamics VSports手机版. CAP enhances the recharging of actin monomers with ATP antagonistically to ADF/cofilin, and also promotes the severing of actin filaments in cooperation with ADF/cofilin. Self-oligomerization and binding to other proteins regulate activities and localization of CAP. CAP has crucial roles in cell signaling, development, vesicle trafficking, cell migration and muscle sarcomere assembly. This Commentary discusses the recent advances in our understanding of the functions of CAP and its implications as an important regulator of actin cytoskeletal dynamics, which are involved in various cellular activities. .

Keywords: ADF/cofilin; Actin turnover; Cyclase-associated protein; Nucleotide exchange; Severing. V体育安卓版.

PubMed Disclaimer

"V体育官网" Figures

Fig. 1.
Fig. 1.
Structure of CAP. (A) Domain organization of CAP and C-CAP (CAP in protozoans). Representative interaction partners and actin-regulatory functions are shown below functional domains. (B,C) Ribbon diagram of the structures of the helical folded domain (HFD) (Protein Data Bank accession number 1S0P) (B) and β-sheet/β-helix (CARP) domain (Protein Data Bank accession number 1K8F) (C). Structures of monomers (top) and dimers (bottom) are shown. Locations of N- and C-termini are indicated. The molecular graphics were produced with PyMOL (Schrödinger, LLC).
Fig. 2.
Fig. 2.
Phylogenetic tree of CAPs in eukaryotes. Amino acid sequences of CAP-related proteins from representative organisms were analyzed by Clustal W (Thompson et al., 1994) and classified as shown on the left. See supplementary material Table S1 for database accession numbers sequences.
Fig. 3.
Fig. 3.
Regulation of actin filament dynamics by CAP, ADF/cofilin, profilin and AIP1. CAP competes with ADF/cofilin for binding to G-actin (right) and promotes its nucleotide exchange (top). CAP also promotes severing of ADF/cofilin-bound actin filaments (bottom). These activities are similar to those exerted by profilin and AIP1. ADF/cofilin cooperatively binds to actin filaments and severs them at the boundary between ADF/cofilin-bound and the bare segments (Elam et al., 2013). Note that the molecular organization of the CAP oligomer is hypothetical. Also note that CAP binds to actin monomers in an oligomeric form but, for simplicity, only a monomeric CAP is shown as a G-actin-bound form.
Fig. 4.
Fig. 4.
Biological functions of CAP.
See this image and copyright information in PMC

References

    1. Agrawal P. B., Greenleaf R. S., Tomczak K. K., Lehtokari V. L., Wallgren-Pettersson C., Wallefeld W., Laing N. G., Darras B. T., Maciver S. K., Dormitzer P. R. et al.(2007). Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2. Am. J. Hum. Genet. 80, 162–167 10.1086/510402 - DOI (V体育安卓版) - PMC - PubMed
    1. Agrawal P. B., Joshi M., Savic T., Chen Z., Beggs A. H. (2012). Normal myofibrillar development followed by progressive sarcomeric disruption with actin accumulations in a mouse Cfl2 knockout demonstrates requirement of cofilin-2 for muscle maintenance. Hum. Mol. Genet. 21, 2341–2356 10.1093/hmg/dds053 - DOI (V体育平台登录) - PMC - PubMed
    1. Amberg D. C., Basart E., Botstein D. (1995). Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 2, 28–35 10.1038/nsb0195-28 - DOI - PubMed
    1. Balcer H. I., Goodman A. L., Rodal A. A., Smith E., Kugler J., Heuser J. E., Goode B. L. (2003). Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aip1. Curr. Biol. 13, 2159–2169 10.1016/j.cub.2003.11.051 - DOI - PubMed
    1. Barrero R. A., Umeda M., Yamamura S., Uchimiya H. (2002). Arabidopsis CAP regulates the actin cytoskeleton necessary for plant cell elongation and division. Plant Cell 14, 149–163 10.1105/tpc.010301 - "V体育ios版" DOI - PMC - PubMed

LinkOut - more resources (V体育ios版)