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Gene Review

Capg  -  capping protein (actin filament), gelsolin...

Mus musculus

Synonyms: Actin regulatory protein CAP-G, Actin-capping protein GCAP39, Macrophage-capping protein, Mbh1, Myc basic motif homolog 1, ...
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High impact information on Capg

  • The coexistence of gCap39 with gelsolin should allow precise regulation of actin assembly at the leading edge of the cell [1].
  • However, gCap39 does not sever actin filaments and can respond to Ca2+ and PPI transients independently, under conditions in which gelsolin is ineffective [1].
  • Examination of Mbh1 localization in 3T3 fibroblasts by indirect immunofluorescence reveals a larger cell population showing diffuse staining, and a smaller population exhibiting a distinct nuclear stain [2].
  • Embedded within the amino acid sequence encoded by mbh1 is a region distantly related to the basic/helix-loop-helix (B/HLH) DNA-binding motif and a potential nuclear localization signal [2].
  • Translation of mbh1 RNA in rabbit reticulocyte extracts produces an approximately 45 kd protein capable of binding actin-coupled agarose beads in vitro in a Ca2(+)-dependent manner [2].

Biological context of Capg

  • Western analysis corroborates this intracellular localization and indicates that total cellular levels and localization of Mbh1 are not affected by the cell growth state [2].
  • The phosphorylation state of gCap39 in cells is therefore regulated by a balance between kinases and okadaic acid-sensitive phosphatases, and phosphorylation sites containing threonines appear to be particularly sensitive to the phosphatases [3].
  • Nuclear gCap39 redistributes throughout the cytoplasm during mitosis and is excluded from regions containing chromosomes [4].

Anatomical context of Capg

  • Purification and expression of gCap39. An intracellular and secreted Ca2(+)-dependent actin-binding protein enriched in mononuclear phagocytes [5].
  • When an expression vector containing the gCap39 coding region was transfected into COS cells, high levels of gCap39 were found in both the cells and conditioned media, whereas annexins were only present in the cells. gCap39 could also be purified from human plasma where it appeared to be a minor component [5].
  • We found that gCap39 is very abundant in macrophages (accounting for 0.6% of total macrophage proteins), and is present in 12-fold molar excess to gelsolin [4].
  • Both proteins are highly induced during differentiation of the promyelocytic leukemia cell line into macrophages. gCap39 is less abundant in fibroblasts (0.04% total proteins) and is present in equal molar ratio to gelsolin [4].

Other interactions of Capg


  1. gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein. Yu, F.X., Johnston, P.A., Südhof, T.C., Yin, H.L. Science (1990) [Pubmed]
  2. Mbh 1: a novel gelsolin/severin-related protein which binds actin in vitro and exhibits nuclear localization in vivo. Prendergast, G.C., Ziff, E.B. EMBO J. (1991) [Pubmed]
  3. gCap39 is phosphorylated. Stimulation by okadaic acid and preferential association with nuclei. Onoda, K., Yin, H.L. J. Biol. Chem. (1993) [Pubmed]
  4. gCap39 is a nuclear and cytoplasmic protein. Onoda, K., Yu, F.X., Yin, H.L. Cell Motil. Cytoskeleton (1993) [Pubmed]
  5. Purification and expression of gCap39. An intracellular and secreted Ca2(+)-dependent actin-binding protein enriched in mononuclear phagocytes. Johnston, P.A., Yu, F.X., Reynolds, G.A., Yin, H.L., Moomaw, C.R., Slaughter, C.A., Südhof, T.C. J. Biol. Chem. (1990) [Pubmed]
  6. Inflammatory response in white adipose tissue in the non-obese hormone-sensitive lipase null mouse model. Hansson, O., Ström, K., Güner, N., Wierup, N., Sundler, F., Höglund, P., Holm, C. J. Proteome Res. (2006) [Pubmed]
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