ADF/n-cofilin-dependent actin turnover determines platelet formation and sizing Running title: ADF/n-cofilin in platelet production and function
نویسندگان
چکیده
Rudolf Virchow Center, DFG Research Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany Chair of Vascular Medicine, University Hospital, University of Würzburg, 97080 Würzburg, Germany UMR-S949 Inserm-Université de Strasbourg, EFS-Alsace, 67065 Strasbourg, France Hematology Division, Brigham and Women's Hospital, Harvard University, 02115 Boston, USA Division of Electron Microscopy, University of Würzburg, 97074 Würzburg, Germany Institute of Pharmacology and Toxicology, University of Würzburg, 97078 Würzburg, Germany Institute of Genetics, University of Bonn, 53117 Bonn, Germany
منابع مشابه
ADF/n-cofilin-dependent actin turnover determines platelet formation and sizing.
The cellular and molecular mechanisms orchestrating the complex process by which bone marrow megakaryocytes form and release platelets remain poorly understood. Mature megakaryocytes generate long cytoplasmic extensions, proplatelets, which have the capacity to generate platelets. Although microtubules are the main structural component of proplatelets and microtubule sliding is known to drive p...
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ADF/cofilins are essential regulators of actin filament turnover. Several ADF/cofilin isoforms are found in multicellular organisms, but their biological differences have remained unclear. Here we show that three ADF/cofilins exist in mouse and most likely in all other mammalian species. Northern blot, and in situ hybridization analyses demonstrate that cofilin-1 is expressed in most cell types...
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Actin is a regulator of synaptic vesicle mobilization and exocytosis, but little is known about the mechanisms that regulate actin at presynaptic terminals. Genetic data on LIMK1, a negative regulator of actin-depolymerizing proteins of the ADF/cofilin family, suggest a role for ADF/cofilin in presynaptic function. However, synapse physiology is fully preserved upon genetic ablation of ADF in m...
متن کاملRegulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.
Actin depolymerizing factor (ADF)/cofilin enhances turnover of actin filaments by severing and depolymerizing filaments. A number of proteins functionally interact with ADF/cofilin to modulate the dynamics of actin filaments. Actin-interacting protein 1 (AIP1) has emerged as a conserved WD-repeat protein that specifically enhances ADF/cofilin-induced actin dynamics. Interaction of AIP1 with act...
متن کاملUNC-87, a calponin-related protein in C. elegans, antagonizes ADF/cofilin-mediated actin filament dynamics.
Stabilization of actin filaments is critical for supporting actomyosin-based contractility and for maintaining stable cellular structures. Tropomyosin is a well-characterized ubiquitous actin stabilizer that inhibits ADF/cofilin-dependent actin depolymerization. Here, we show that UNC-87, a calponin-related Caenorhabditis elegans protein with seven calponin-like repeats, competes with ADF/cofil...
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