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F-actin capping protein

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F-actin capping protein alpha subunit
solution nmr structure of s100b bound to the high-affinity target peptide trtk-12
Identifiers
SymbolF-actin_cap_A
PfamPF01267
InterProIPR018315
PROSITEPDOC00609
SCOP21izn / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
F-actin capping protein, beta subunit
Identifiers
SymbolF_actin_cap_B
PfamPF01115
InterProIPR001698
PROSITEPDOC00203
SCOP21izn / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the F-actin capping protein is a protein complex which binds in a calcium-independent manner to the fast-growing ends of actin filaments (barbed end), thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrelated subunits: alpha and beta. Neither of the subunits shows sequence similarity to other filament-capping proteins.[1] The alpha subunit is a protein of about 268 to 286 amino acid residues and the beta subunit is approximately 280 amino acids, their sequences are well conserved in eukaryotic species.[2]

The actin filament system, a prominent part of the cytoskeleton in eukaryotic cells, is both a static structure and a dynamic network that can undergo rearrangements: it is thought to be involved in processes such as cell movement and phagocytosis, as well as muscle contraction.[1]

References

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  1. ^ a b Maruyama K, Kurokawa H, Oosawa M, Shimaoka S, Yamamoto H, Ito M, Maruyama K (May 1990). "Beta-actinin is equivalent to Cap Z protein". J. Biol. Chem. 265 (15): 8712–5. doi:10.1016/S0021-9258(19)38947-1. PMID 2341404.
  2. ^ Cooper JA, Caldwell JE, Gattermeir DJ, Torres MA, Amatruda JF, Casella JF (1991). "Variant cDNAs encoding proteins similar to the alpha subunit of chicken CapZ". Cell Motil. Cytoskeleton. 18 (3): 204–14. doi:10.1002/cm.970180306. PMID 1711931.
This article incorporates text from the public domain Pfam and InterPro: IPR018315
This article incorporates text from the public domain Pfam and InterPro: IPR001698