A5071801805- Cardiomyopathy and Myosin Studies
- Signaling Pathways in Disease
- Advanced Fluorescence Microscopy Techniques
- Advanced Electron Microscopy Techniques and Applications
- Nuclear Structure and Function
- RNA and protein synthesis mechanisms
- Cellular Mechanics and Interactions
- Muscle Physiology and Disorders
- Enzyme Structure and Function
- RNA Research and Splicing
- Protein Structure and Dynamics
Southern University of Science and Technology
2022-2024
Shenzhen University
2024
Abstract Myosin VI is the only molecular motor that moves towards minus end along actin filaments. Numerous cellular processes require myosin and tight regulations of motor’s activity. Defects in activity are known to cause genetic diseases such as deafness cardiomyopathy. However, mechanisms underlying regulation remain elusive. Here, we determined high-resolution cryo-electron microscopic structure its autoinhibited state. Our reveals adopts a compact, monomeric conformation via extensive...
As the prototype of unconventional myosin motor family, Va (MyoVa) transport cellular cargos along actin filaments in diverse processes. The off-duty MyoVa adopts a closed and autoinhibited state, which can be relieved by cargo binding. molecular mechanisms governing autoinhibition activation remain unclear. Here, we report cryo-electron microscopy structure two full-length, heavy chains complex with 12 calmodulin light at 4.78-Å resolution. triangular multiple intra- interpolypeptide chain...
SH3 domains are common protein binding modules. The target sequence of is usually a proline-rich motif (PRM) containing minimal "PxxP" sequence. mechanism how different specifically choose their targets from vast PxxP-containing sequences still not very clear, as many reported SH3/PRM interactions weak and promiscuous. Here, we identified the domain ASAP1 to PRM MICAL1 with sub-μM affinity, determined crystal structure ASAP1-SH3 MICAL1-PRM complex. Our structural biochemical analyses...
MICAL proteins represent a unique family of actin regulators crucial for synapse development, membrane trafficking, and cytokinesis. Unlike classical regulators, MICALs catalyze the oxidation specific residues within filaments to induce robust filament disassembly. The potent activity requires tight control prevent extensive damage cytoskeleton. However, molecular mechanism governing MICALs' regulation remains elusive. Here, we report cryo-EM structure MICAL1 in autoinhibited state,...
<title>Abstract</title> MICAL (Molecule Interacting with CasL) proteins represent a unique family of actin regulators crucial for synapse development, membrane trafficking, and cytokinesis. Unlike classical regulators, possess enzymatic activity, catalyzing the oxidation specific residues within filaments to induce robust filament severing. The potent activity requires tight control prevent extensive damage cytoskeleton. Due limited structural information on full-length proteins, molecular...