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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Christophe LE CLAINCHE & Louis RENAULT : Dynamique du cytosquelette et motilité

pubmed : ( ( (( "le clainche ...

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NCBI : db=pubmed ; Term=( ( (( "Le clainche C"[author] OR "Renault L"[author] OR "DAVID V"[author] OR "LAI TL"[author] OR "HENRIOT V"[author] OR ("WANG H"[author] AND "Le clainche C"[author]) OR ("FELLOUS S"[author] AND "RENAULT L"[author]) ) AND "2014/01/01"[Date - Publication] : "3000"[Date - Publication] ) OR ( "2014/01/01"[Date - Publication] : "2018/01/01"[Date - Publication] AND ("Carlier MF"[author] OR (("Ciobanasu C"[author] OR "Faivre B"[author]) AND "Le clainche C"[author]) OR (("PERNIER J"[author] OR "MONTAVILLE P"[author] OR "Shekhar S"[author] OR "Kühn S"[author] OR "Guichard B"[author] OR "Jiao Y"[author] OR "COMPPER C"[author]) AND "Carlier MF"[author]) ) ) ) AND ("Laboratoire d’Enzymologie et Biochimie Structurales"[Affiliation] OR I2BC[Affiliation] OR "Institute for Integrative Biology of the Cell"[Affiliation] ) OR ("LAI TL"[author] AND "2016/01/01"[Date - Publication] : "3000"[Date - Publication] AND "iBiTec-s"[Affiliation]) )

Articles syndiqués

  • Enhanced Depolymerization of Actin Filaments by ADF/Cofilin and Monomer Funneling by Capping Protein Cooperate to Accelerate Barbed-End Growth.

    20 juin, par Shekhar S, Carlier MF
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    Enhanced Depolymerization of Actin Filaments by ADF/Cofilin and Monomer Funneling by Capping Protein Cooperate to Accelerate Barbed-End Growth.

    Curr Biol. 2017 Jun 09;:

    Authors: Shekhar S, Carlier MF

    Abstract
    A living cell's ability to assemble actin filaments in intracellular motile processes is directly dependent on the availability of polymerizable actin monomers, which feed polarized filament growth [1, 2]. Continued generation of the monomer pool by filament disassembly is therefore crucial. Disassemblers like actin depolymerizing factor (ADF)/cofilin and filament cappers like capping protein (CP) are essential agonists of motility [3-8], but the exact molecular mechanisms by which they accelerate actin polymerization at the leading edge and filament turnover has been debated for over two decades [9-12]. Whereas filament fragmentation by ADF/cofilin has long been demonstrated by total internal reflection fluorescence (TIRF) [13, 14], filament depolymerization was only inferred from bulk solution assays [15]. Using microfluidics-assisted TIRF microscopy, we provide the first direct visual evidence of ADF's simultaneous severing and rapid depolymerization of individual filaments. Using a conceptually novel assay to directly visualize ADF's effect on a population of pre-assembled filaments, we demonstrate how ADF's enhanced pointed-end depolymerization causes an increase in polymerizable actin monomers, thus promoting faster barbed-end growth. We further reveal that ADF-enhanced depolymerization synergizes with CP's long-predicted "monomer funneling" [16] and leads to skyrocketing of filament growth rates, close to estimated lamellipodial rates. The "funneling model" hypothesized, on thermodynamic grounds, that at high enough extent of capping, the few non-capped filaments transiently grow much faster [15], an effect proposed to be very important for motility. We provide the first direct microscopic evidence of monomer funneling at the scale of individual filaments. These results significantly enhance our understanding of the turnover of cellular actin networks.

    PMID: 28625780 [PubMed - as supplied by publisher]

  • Crystal structure and redox properties of a novel cyanobacterial heme protein with a His/Cys heme axial ligation and a Per-Arnt-Sim (PAS)-like domain.

    22 avril, par Motomura T, Suga M, Hienerwadel R, Nakagawa A, Lai TL, Nitschke W, Kuma T, Sugiura M, Boussac A, Shen JR
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    Crystal structure and redox properties of a novel cyanobacterial heme protein with a His/Cys heme axial ligation and a Per-Arnt-Sim (PAS)-like domain.

    J Biol Chem. 2017 Jun 09;292(23):9599-9612

    Authors: Motomura T, Suga M, Hienerwadel R, Nakagawa A, Lai TL, Nitschke W, Kuma T, Sugiura M, Boussac A, Shen JR

    Abstract
    Photosystem II catalyzes light-induced water oxidation leading to the generation of dioxygen indispensable for sustaining aerobic life on Earth. The Photosystem II reaction center is composed of D1 and D2 proteins encoded by psbA and psbD genes, respectively. In cyanobacteria, different psbA genes are present in the genome. The thermophilic cyanobacterium Thermosynechococcus elongatus contains three psbA genes: psbA1, psbA2, and psbA3, and a new c-type heme protein, Tll0287, was found to be expressed in a strain expressing the psbA2 gene only, but the structure and function of Tll0287 are unknown. Here we solved the crystal structure of Tll0287 at a 2.0 Å resolution. The overall structure of Tll0287 was found to be similar to some kinases and sensor proteins with a Per-Arnt-Sim-like domain rather than to other c-type cytochromes. The fifth and sixth axial ligands for the heme were Cys and His, instead of the His/Met or His/His ligand pairs observed for most of the c-type hemes. The redox potential, E½, of Tll0287 was -255 ± 20 mV versus normal hydrogen electrode at pH values above 7.5. Below this pH value, the E½ increased by ≈57 mV/pH unit at 15 °C, suggesting the involvement of a protonatable group with a pKred = 7.2 ± 0.3. Possible functions of Tll0287 as a redox sensor under microaerobic conditions or a cytochrome subunit of an H2S-oxidizing system are discussed in view of the environmental conditions in which psbA2 is expressed, as well as phylogenetic analysis, structural, and sequence homologies.

    PMID: 28428249 [PubMed - indexed for MEDLINE]