Dorit Hanein · University of California, Santa Barbara · PhdFit
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Dr. Sarah Chen
Stanford · NLP & interpretability
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Dorit Hanein
· Professor of Bioengineering Professor of Chemistry and BiochemistryVerified
University of California, Santa Barbara · Bioengineering
Dorit Hanein is a Professor of Bioengineering and Chemistry and Biochemistry at UC Santa Barbara. Her research focuses on exploring the complexities of macromolecular machines that drive biological processes, including immune responses, sensory perceptions, healing mechanisms, and the processes of maturation and aging. She leads the Hanein Lab, which utilizes advanced cryogenic light and electron microscopes to obtain quantitative representations of biological structures at the atomic scale, allowing for the observation of mechanical alterations within complex three-dimensional environments.
Actin, a highly conserved and ubiquitous eukaryotic protein, underlies essential cellular processes including motility, shape maintenance and muscle contraction. Its dynamic transition between monomeric and filamentous states is powered by ATP hydrolysis, which undergoes structural rearrangements that accelerate turnover in filaments and serve as a measure of filament aging. A wide range of actin binding proteins (ABPs) regulate polymerization, depolymerization, and network organization. Recent high resolution cryo-EM and cryo-ET studies have revealed detailed structures of actin, its isoforms, and ABP complexes, including their organization in cells, deepening our understanding of actin function in health and disease.
International Journal of Molecular Sciences · 2024-07-11 · 1 citations
articleOpen accessCorresponding
Common challenges in cryogenic electron microscopy, such as orientation bias, conformational diversity, and 3D misclassification, complicate single particle analysis and lead to significant resource expenditure. We previously introduced an in silico method using the maximum Feret diameter distribution, the Feret signature, to characterize sample heterogeneity of disc-shaped samples. Here, we expanded the Feret signature methodology to identify preferred orientations of samples containing arbitrary shapes with only about 1000 particles required. This method enables real-time adjustments of data acquisition parameters for optimizing data collection strategies or aiding in decisions to discontinue ineffective imaging sessions. Beyond detecting preferred orientations, the Feret signature approach can serve as an early-warning system for inconsistencies in classification during initial image processing steps, a capability that allows for strategic adjustments in data processing. These features establish the Feret signature as a valuable auxiliary tool in the context of single particle analysis, significantly accelerating the structure determination process.
Actin filament assembly and the regulation of its mechanical properties are fundamental processes essential for eukaryotic cell function. Residue E167 in vertebrate actins forms an inter-subunit salt bridge with residue K61 of the adjacent subunit. Saccharomyces cerevisiae actin filaments are more flexible than vertebrate filaments and have an alanine at this position (A167). Substitution of this alanine for a glutamic acid (A167E) confers Saccharomyces cerevisiae actin filaments with salt-dependent stiffness similar to vertebrate actins. We developed an optimized cryogenic electron microscopy workflow refining sample preparation and vitrification to obtain near-atomic resolution structures of wild-type and A167E mutant Saccharomyces cerevisiae actin filaments. The difference between these structures allowed us to pinpoint the potential binding site of a filament-associated cation that controls the stiffness of the filaments in vertebrate and A167E Saccharomyces cerevisiae actins. Through an analysis of previously published high-resolution reconstructions of vertebrate actin filaments, along with a newly determined high-resolution vertebrate actin structure in the absence of potassium, we identified a unique peak near residue 167 consistent with the binding of a magnesium ion. Our findings show how magnesium can contribute to filament stiffening by directly bridging actin subunits and allosterically affecting the orientation of the DNase-I binding loop of actin, which plays a regulatory role in modulating actin filament stiffness and interactions with regulatory proteins.
White Rose Research Online (University of Leeds, The University of Sheffield, University of York) · 2024-10-16
articleOpen access
In September 2023, the two largest bioimaging networks in the Americas, Latin America Bioimaging (LABI) and BioImaging North America (BINA), came together during a 1-week meeting in Mexico. This meeting provided opportunities for participants to interact closely with decision-makers from imaging core facilities across the Americas. The meeting was held in a hybrid format and attended in-person by imaging scientists from across the Americas, including Canada, the United States, Mexico, Colombia, Peru, Argentina, Chile, Brazil and Uruguay. The aims of the meeting were to discuss progress achieved over the past year, to foster networking and collaborative efforts among members of both communities, to bring together key members of the international imaging community to promote the exchange of experience and expertise, to engage with industry partners, and to establish future directions within each individual network, as well as common goals. This meeting report summarises the discussions exchanged, the achievements shared, and the goals set during the LABIxBINA2023: Bioimaging across the Americas meeting.
