Benjamin Barsi‐Rhyne

ORCID: 0000-0002-6610-1766
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About
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Research Areas
  • Receptor Mechanisms and Signaling
  • Genetics, Aging, and Longevity in Model Organisms
  • Neuropeptides and Animal Physiology
  • Circadian rhythm and melatonin
  • SARS-CoV-2 and COVID-19 Research
  • Protein Kinase Regulation and GTPase Signaling
  • Molecular Communication and Nanonetworks
  • Photoreceptor and optogenetics research
  • Axon Guidance and Neuronal Signaling
  • Monoclonal and Polyclonal Antibodies Research
  • SARS-CoV-2 detection and testing
  • Phosphodiesterase function and regulation
  • Advancements in Semiconductor Devices and Circuit Design
  • Neurobiology and Insect Physiology Research
  • Nanowire Synthesis and Applications
  • Gene Regulatory Network Analysis
  • Virus-based gene therapy research
  • Single-cell and spatial transcriptomics
  • Mass Spectrometry Techniques and Applications
  • Pancreatic function and diabetes
  • Microtubule and mitosis dynamics
  • Advanced Biosensing Techniques and Applications
  • Advanced biosensing and bioanalysis techniques
  • CRISPR and Genetic Engineering
  • Neuroendocrine regulation and behavior

University of California, San Francisco
2016-2023

San Jose State University
2011-2019

University at Buffalo, State University of New York
2018

Michael Schoof Bryan Faust Reuben A. Saunders Smriti Sangwan Veronica V. Rezelj and 95 more Nick Hoppe Morgane Boone Christian B. Billesbølle Cristina Puchades Caleigh M. Azumaya Huong T. Kratochvil M. Zimanyi Ishan Deshpande Jiahao Liang Sasha Dickinson Henry C. Nguyen Cynthia M. Chio Gregory E. Merz Michael C. Thompson Devan Diwanji Kaitlin Schaefer Aditya Anand Niv Dobzinski Beth Shoshana Zha Camille R. Simoneau Kristoffer E. Leon Kris M. White Un Seng Chio Meghna Gupta Mingliang Jin Fei Li Yanxin Liu Kaihua Zhang David Bulkley Ming Sun Amber M. Smith Alexandrea N. Rizo Frank R. Moss Axel F. Brilot Sergei Pourmal Raphael Trenker Thomas H. Pospiech Sayan Gupta Benjamin Barsi‐Rhyne Vladislav Belyy Andrew W. Barile-Hill Silke Nock Yuwei Liu Nevan J. Krogan Corie Y. Ralston Danielle L. Swaney Adolfo Garcı́a-Sastre Mélanie Ott Marco Vignuzzi Peter Walter Aashish Manglik Caleigh M. Azumaya Cristina Puchades Ming Sun Julian R. Braxton Axel F. Brilot Meghna Gupta Fei Li Kyle E. Lopez Arthur A. Melo Gregory E. Merz Frank R. Moss Joana Paulino Thomas H. Pospiech Sergei Pourmal Alexandrea N. Rizo Amber M. Smith Paul V. Thomas Feng Wang Zanlin Yu Miles Sasha Dickinson Henry C. Nguyen Daniel Asarnow Melody G. Campbell Cynthia M. Chio Un Seng Chio Devan Diwanji Bryan Faust Meghna Gupta Nick Hoppe Mingliang Jin Junrui Li Yanxin Liu Gregory E. Merz Smriti Sangwan Tsz Kin Martin Tsui Raphael Trenker Donovan Trinidad Eric Tse Kaihua Zhang Fengbo Zhou Nadia Herrera Huong T. Kratochvil Ursula Schulze‐Gahmen Michael C. Thompson

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus enters host cells via an interaction between its Spike protein and the cell receptor angiotensin-converting enzyme (ACE2). By screening a yeast surface-displayed library of synthetic nanobody sequences, we developed nanobodies that disrupt ACE2. Cryo-electron microscopy (cryo-EM) revealed one nanobody, Nb6, binds in fully inactive conformation with binding domains locked into their inaccessible down state, incapable...

10.1126/science.abe3255 article EN cc-by Science 2020-11-06

In addition to the popular method of fluorescent protein fusion, live cell imaging has now seen more and application epitope tags. The small size these tags may reduce functional perturbation enable signal amplification. To address their background issue, we adapt self-complementing split proteins as for labelling. two tags, GFP11 sfCherry11 are derived from eleventh β-strand super-folder GFP sfCherry, respectively. FP11-tags enables a cost-effective scalable way insert them into endogenous...

10.1038/ncomms11046 article EN cc-by Nature Communications 2016-03-18

Binding of arrestin to phosphorylated G protein-coupled receptors (GPCRs) is crucial for modulating signaling. Once internalized, some GPCRs remain complexed with β-arrestins, while others interact only transiently; this difference affects GPCR signaling and recycling. Cell-based in vitro biophysical assays reveal the role membrane phosphoinositides (PIPs) β-arrestin recruitment GPCR-β-arrestin complex dynamics. We find that broadly stratify into two groups, one requires PIP binding does...

10.1016/j.cell.2022.10.018 article EN cc-by-nc-nd Cell 2022-11-01

ABSTRACT Without an effective prophylactic solution, infections from SARS-CoV-2 continue to rise worldwide with devastating health and economic costs. gains entry into host cells via interaction between its Spike protein the cell receptor angiotensin converting enzyme 2 (ACE2). Disruption of this confers potent neutralization viral entry, providing avenue for vaccine design therapeutic antibodies. Here, we develop single-domain antibodies (nanobodies) that potently disrupt ACE2. By screening...

10.1101/2020.08.08.238469 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-08-10

Abstract Background An essential stage of neural development involves the assembly circuits via formation inter-neuronal connections. Early steps in circuit formation, including cell migration, axon guidance, and localization synaptic components, are well described. However, upon reaching their target region, most neurites still contact many potential partners. In order to assemble functional circuits, it is critical that within this group cells, neurons identify form connections only with...

10.1186/1749-8104-6-28 article EN cc-by Neural Development 2011-06-10

Abstract cGMP plays a role in sensory signaling and plasticity by regulating ion channels, phosphodiesterases, kinases. Studies that primarily used genetic biochemical tools suggest is spatiotemporally regulated multiple modalities. FRET- GFP-based sensors were developed to visualize primary cell culture Caenorhabditis elegans corroborate these findings. While FRET-based sensor has been an intact animal cGMP, the requirement of emission system limits its ability be on own as well with other...

10.1534/genetics.119.302392 article EN cc-by Genetics 2019-07-23

β-Arrestins are master regulators of cellular signaling that operate by desensitizing ligand-activated G-protein-coupled receptors (GPCRs) at the plasma membrane and promoting their subsequent endocytosis. The endocytic activity β-arrestins is ligand dependent, triggered GPCR binding, increasingly recognized to have a multitude downstream trafficking consequences specifically programmed bound GPCR. However, only one biochemical ‘mode’ for GPCR-mediated triggering presently known –...

10.7554/elife.81563 article EN cc-by eLife 2022-10-17

β-arrestins play a key role in G protein-coupled receptor (GPCR) internalization, trafficking, and signaling. Whether act independently of protein-mediated signaling has not been fully elucidated. Studies using genome-editing approaches revealed that whereas proteins are essential for mitogen-activated protein kinase activation by GPCRs., more prominent signal compartmentalization. However, the absence proteins, GPCRs may activate β-arrestins, thereby limiting ability to distinguish from...

10.1016/j.jbc.2023.105293 article EN cc-by Journal of Biological Chemistry 2023-09-27

The organization of neurons and the maintenance that arrangement are critical to brain function. Failure these processes in humans can lead severe birth defects, mental retardation, epilepsy. Several kinesins have been shown play important roles cell migration vertebrate systems, but few upstream downstream pathway members identified. Here, we utilize genetic model organism Caenorhabditis elegans elucidate by which C. Kinesin-1 Heavy Chain (KHC)/KIF5 ortholog UNC-116 functions maintain...

10.1534/genetics.113.149310 article EN Genetics 2013-03-09

Summary Binding of arrestin to phosphorylated G protein-coupled receptors (GPCRs) is crucial for modulating signaling. Once internalized some GPCRs may complex with arrestin, while others interact transiently; this difference affects receptor signaling and recycling. Cell-based in vitro biophysical assays reveal the role membrane phosphoinositides (PIPs) recruitment GPCR-arrestin dynamics. We find that broadly stratify into two groups, one requiring PIP-binding does not. Plasma PIPs...

10.1101/2021.10.09.463790 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-10-10

Abstract cGMP is a ubiquitous second messenger that plays role in sensory signaling and plasticity through its regulation of ion channels kinases. Previous studies primarily used genetic biochemical tools suggest spatiotemporally regulated multiple modalities, including light, heat, gases, salt odor. FRET- GFP-based sensors were developed to visualize primary cell culture Caenorhabditis elegans corroborate these findings. While FRET-based sensor has been an intact animal cGMP, the...

10.1101/433425 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2018-10-02

Binding of arrestin to phosphorylated G protein-coupled receptors (GPCRs) is crucial for gating signaling. Once internalized some GPCRs remain stably associated with arrestin, while others interact transiently; this difference affects signaling and recycling behaviors these GPCRs. Using cell-based in vitro biophysical assays we examined the role membrane phosphoinositides (PIPs) recruitment GPCR-arrestin complex dynamics. We find that broadly stratify into two groups, one which requires...

10.1096/fasebj.2022.36.s1.r6320 article EN The FASEB Journal 2022-05-01

Abstract β-arrestins are master regulators of cellular signaling that operate by desensitizing ligand-activated G protein-coupled receptors (GPCRs) at the plasma membrane and promoting their subsequent endocytosis. The endocytic activity is ligand-dependent, triggered GPCR binding, increasingly recognized to have a multitude downstream trafficking consequences specifically programmed bound GPCR. However, only one biochemical ‘mode’ for GPCR-mediated triggering presently known– displacement...

10.1101/2022.07.13.499995 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2022-07-15
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