alpha smooth muscle Actin Recombinant Antibody [SY02-64] - Rat IgG1 (Chimeric)

Function

All eukaryotic cells express Actin, which often constitutes as much as 50% of total cellular protein. Actin filaments can form both stable and labile structures and are crucial components of microvilli and the contractile apparatus of muscle cells. While lower eukaryotes, such as yeast, have only one Actin gene, higher eukaryotes have several isoforms encoded by a family of genes. At least six types of Actin are present in mammalian tissues and fall into three classes. α-Actin expression is limited to various types of muscle, whereas β-Actin and γ-Actin are the principle constituents of filaments in other tissues. Members of the small GTPase family regulate the organization of the Actin cytoskeleton. Rho controls the assembly of Actin stress fibers and focal adhesion. Rac regulates Actin filament accumulation at the plasma membrane. Cdc42 stimulates formation of filopodia.

Background References

1. Izumi D et al. CXCL12/CXCR4 activation by cancer-associated fibroblasts promotes integrin 1 clustering and invasiveness in gastric cancer. Int J Cancer 138:1207-19 (2016).

2. Chung SI et al. Development of a transgenic mouse model of hepatocellular carcinoma with a liver fibrosis background. BMC Gastroenterol 16:13 (2016).

Sequence Similarity

Belongs to the actin family.

Post-translational Modification

Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization.; Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration.; Methylated at His-75 by SETD3.; (Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-52 of one monomer and Glu-272 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding. The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners.

Subcellular Location

Cytoplasm.

UNIPROT

SwissProt: P62736 Human

SwissProt: P62737 Mouse

SwissProt: P62738 Rat

Synonyms