ACTG1

5JLH7111465ENSG00000184009ENSMUSG00000062825P63261P63260NM_001199954NM_001614NM_009609NM_001313923NP_001186883NP_001605NP_001300852NP_033739Gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells. Mutations in ACTG1 have been associated with nonsyndromic hearing loss and Baraitser-Winter syndrome, as well as susceptibility of adolescent patients to vincristine toxicity.1atn: Atomic structure of the actin:DNASE I complex1c0f: CRYSTAL STRUCTURE OF DICTYOSTELIUM CAATP-ACTIN IN COMPLEX WITH GELSOLIN SEGMENT 11c0g: CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)1d4x: Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.1dej: CRYSTAL STRUCTURE OF A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 646: Q228K/T229A/A230Y/A231K/S232E/E360H) IN COMPLEX WITH HUMAN GELSOLIN SEGMENT 11eqy: COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 11esv: COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 11h1v: GELSOLIN G4-G6/ACTIN COMPLEX1hlu: STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE1ijj: THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBIT SKELETAL MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 A RESOLUTION1j6z: UNCOMPLEXED ACTIN1kxp: CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN IN COMPLEX WITH SKELETAL ACTIN1lcu: Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution1lot: CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING PROTEIN1m8q: Molecular Models of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle1ma9: Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin1mdu: Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)1mvw: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1nlv: Crystal Structure Of Dictyostelium Discoideum Actin Complexed With Ca ATP And Human Gelsolin Segment 11nm1: Crystal Structure of D. Dicsoideum Actin Complexed With Gelsolin Segment 1 and Mg ATP at 1.8 A Resolution1nmd: Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP1nwk: CRYSTAL STRUCTURE OF MONOMERIC ACTIN IN THE ATP STATE1o18: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1o19: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1o1a: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1o1b: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1o1c: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1o1d: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1o1e: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1o1f: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1o1g: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE1p8z: Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu1561qz5: Structure of rabbit actin in complex with kabiramide C1qz6: Structure of rabbit actin in complex with jaspisamide A1rdw: Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer1rfq: Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer1rgi: Crystal structure of gelsolin domains G1-G3 bound to actin1s22: Absolute Stereochemistry of Ulapualide A1sqk: CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN1t44: Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation1wua: The structure of Aplyronine A-actin complex1y64: Bni1p Formin Homology 2 Domain complexed with ATP-actin1yxq: Crystal structure of actin in complex with swinholide A2a3z: Ternary complex of the WH2 domain of WASP with Actin-DNAse I2a40: Ternary complex of the WH2 domain of WAVE with Actin-DNAse I2a41: Ternary complex of the WH2 Domain of WIP with Actin-DNAse I2a42: Actin-DNAse I Complex2a5x: Crystal Structure of a Cross-linked Actin Dimer2asm: Structure of Rabbit Actin In Complex With Reidispongiolide A2aso: Structure of Rabbit Actin In Complex With Sphinxolide B2asp: Structure of Rabbit Actin In Complex With Reidispongiolide C2btf: THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN2d1k: Ternary complex of the WH2 domain of mim with actin-dnase I2ff3: Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin2ff6: Crystal structure of Gelsolin domain 1:ciboulot domain 2 hybrid in complex with actin2fxu: X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.2gwj: SpvB ADP-ribosylated actin: hexagonal crystal form2gwk: SpvB ADP-ribosylated actin: orthorhombic crystal form2hf3: Crystal structure of monomeric Actin in the ADP bound state2hf4: Crystal structure of Monomeric Actin in its ATP-bound state2hmp: Uncomplexed actin cleaved with protease ECP322oan: Structure of oxidized beta-actin2q1n: Actin Dimer Cross-linked Between Residues 41 and 3742q31: Actin Dimer Cross-linked Between Residues 41 and 374 and proteolytically cleaved by subtilisin between residues 47 and 48.2q36: Actin Dimer Cross-linked between Residues 191 and 374 and complexed with Kabiramide C Gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells. Mutations in ACTG1 have been associated with nonsyndromic hearing loss and Baraitser-Winter syndrome, as well as susceptibility of adolescent patients to vincristine toxicity. Human gamma-actin is 41.8 kDa in molecular weight and 375 amino acids in length. Actins are highly conserved proteins that are involved in various types of cell motility, and maintenance of the cytoskeleton. In vertebrates, three main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the sarcomere contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. Actin, gamma 1, encoded by this gene, is found in non-muscle cells in the cytoplasm, and in muscle cells at costamere structures, or transverse points of cell-cell adhesion that run perpendicular to the long axis of myocytes. In myocytes, sarcomeres adhere to the sarcolemma via costameres, which align at Z-discs and M-lines. The two primary cytoskeletal components of costameres are desmin intermediate filaments and gamma-actin microfilaments. It has been shown that gamma-actin interacting with another costameric protein dystrophin is critical for costameres forming mechanically strong links between the cytoskeleton and the sarcolemmal membrane. Additional studies have shown that gamma-actin colocalizes with alpha-actinin and GFP-labeled gamma actin localized to Z-discs, whereas GFP-alpha-actin localized to pointed ends of thin filaments, indicating that gamma actin specifically localizes to Z-discs in striated muscle cells. During development of myocytes, gamma actin is thought to play a role in the organization and assembly of developing sarcomeres, evidenced in part by its early colocalization with alpha-actinin. Gamma-actin is eventually replaced by sarcomeric alpha-actin isoforms, with low levels of gamma-actin persisting in adult myocytes which associate with Z-disc and costamere domains. Insights into the function of gamma-actin in muscle have come from studies employing transgenesis. In a skeletal muscle-specific knockout of gamma-actin in mice, these animals showed no detectable abnormalities in development; however, knockout mice showed muscle weakness and fiber necrosis, along with decreased isometric twitch force, disrupted intrafibrillar and interfibrillar connections among myocytes, and myopathy. An autosomal dominant mutation in ACTG1 in the DFNA20/26 locus at 17q25-qter was identified in patients with hearing loss. A Thr278Ile mutation was identified in helix 9 of gamma-actin protein, which is predicted to alter protein structure. This study identified the first disease causing mutation in gamma-actin and underlies the importance of gamma-actin as structural elements of the inner ear hair cells. Since then, other ACTG1 mutations have been linked to nonsyndromic hearing loss, including Met305Thr. A missense mutation in ACTG1 at Ser155Phe has also been identified in patients with Baraitser-Winter syndrome, which is a developmental disorder characterized by congenital ptosis, excessively-arched eyebrows, hypertelorism, ocular colobomata, lissencephaly, short stature, seizures and hearing loss. Differential expression of ACTG1 mRNA was also identified in patients with Sporadic Amyotrophic Lateral Sclerosis, a devastating disease with unknown causality, using a sophisticated bioinformatics approach employing Affymetrix long-oligonucleotide BaFL methods.