A5063558144- Cellular Mechanics and Interactions
- Cardiomyopathy and Myosin Studies
- International Relations in Latin America
- Muscle Physiology and Disorders
- Microtubule and mitosis dynamics
- Force Microscopy Techniques and Applications
- Advanced Fluorescence Microscopy Techniques
- Cellular transport and secretion
- International Relations and Foreign Policy
- European Union Policy and Governance
- Global Peace and Security Dynamics
- Heat shock proteins research
- Cell Adhesion Molecules Research
- Advanced Electron Microscopy Techniques and Applications
- International Development and Aid
- Cell Image Analysis Techniques
- 3D Printing in Biomedical Research
- Global trade and economics
- Genomics and Chromatin Dynamics
- Cancer-related Molecular Pathways
- Peptidase Inhibition and Analysis
- Chromatin Remodeling and Cancer
- Ubiquitin and proteasome pathways
- Post-Soviet Geopolitical Dynamics
- Cardiovascular Effects of Exercise
University of Pennsylvania
2016-2025
Suffolk University
2009-2023
Florence (Netherlands)
2023
John Wiley & Sons (United States)
2018
Hudson Institute
2018
University of Virginia
2018
CEA Grenoble
2018
Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2018
Institut de Recherches en Technologies et Sciences pour le Vivant
2018
Chuo University
2018
The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis adenosine 5′-triphosphate (ATP) mechanism that remains be elucidated. Actin modified block polymerization was crystallized in 5′-diphosphate (ADP) state, structure solved 1.54 angstrom resolution. Compared with previous ATP-actin structures from complexes deoxyribonuclease I, profilin, gelsolin, monomeric ADP-actin is characterized marked subdomain 2. successful crystallization...
Significance More than 80% of human proteins are N-terminal (Nt)–acetylated during translation. In contrast, actin, the most abundant protein in cytoplasm animal cells, is Nt-acetylated posttranslationally and following a unique multistep mechanism that has remained poorly characterized. Here, we describe discovery actin’s acetyltransferase (NAT), NAA80. We further demonstrate actin Nt-acetylation plays essential roles filament assembly, cytoskeleton organization, cell motility, resulting...
The barbed and pointed ends of the actin filament (F-actin) are sites growth shrinkage targets capping proteins that block subunit exchange, including CapZ at end tropomodulin end. We describe cryo-electron microscopy structures free capped F-actin. Terminal subunits adopt a "flat" F-actin conformation. binds with minor changes to but major itself. By contrast, "twisted" monomeric (G-actin) Tropomodulin binding forces second into an reveal how differ from middle in these differences control...
Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) is a small and widespread actin-binding motif. In the WASP family, WH2 plays role in filament nucleation by Arp2/3 complex. Here we describe crystal structures of complexes actin with domains WASP, WASP-family verprolin homologous protein, WASP-interacting protein. Despite low sequence identity, shares structural similarity N-terminal portion monomer-sequestering thymosin beta (Tbeta). We show that both inhibit nucleotide...
Initiation of actin polymerization in cells requires nucleation factors. Here we describe an actin-binding protein, leiomodin, that acted as a strong filament nucleator muscle cells. Leiomodin shared two sites with the pointed end-capping protein tropomodulin: flexible N-terminal region and leucine-rich repeat domain. also contained C-terminal extension 150 residues. The smallest fragment activity included extension. enhanced threefold recruited tropomyosin, which weakly stimulated mediated...
The crystal structure at 2.0-Å resolution of an 81-residue N-terminal fragment muscle α-tropomyosin reveals a parallel two-stranded α-helical coiled-coil with remarkable core. high alanine content the molecule is clustered into short regions where local 2-fold symmetry broken by small (≈1.2-Å) axial staggering helices. joining these neighboring segments, helices are in register, gives rise to specific bends molecular axis. We observe such be widely distributed proteins. This asymmetric...
A nucleotide-dependent conformational change regulates actin filament dynamics. Yet, the structural basis of this mechanism remains controversial. The x-ray crystal structure tetramethylrhodamine-5-maleimide-actin with bound AMPPNP, a non-hydrolyzable ATP analog, was determined to 1.85-Å resolution. comparison that ADP, previously under similar conditions, reveals how release nucleotide γ-phosphate sets in motion sequence events leading subdomain 2. side chain Ser-14 catalytic site rotates...
Myosins adjust their power outputs in response to mechanical loads an isoform-dependent manner, resulting ability dynamically adapt a range of motile challenges. Here, we reveal the structural basis for force-sensing based on near-atomic resolution structures one rigor and two ADP-bound states myosin-IB (myo1b) bound actin, determined by cryo-electron microscopy. The are separated 25° rotation lever. lever first ADP state is rotated toward pointed end actin filament forms previously...