Arjun Sangani

ORCID: 0000-0003-1144-6844
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About
Contact & Profiles
Research Areas
  • Cellular transport and secretion
  • Ubiquitin and proteasome pathways
  • RNA Research and Splicing
  • Glycosylation and Glycoproteins Research
  • Photoreceptor and optogenetics research
  • Force Microscopy Techniques and Applications
  • Neuroscience and Neural Engineering
  • Biochemical and Structural Characterization
  • Connexins and lens biology
  • Nanoplatforms for cancer theranostics
  • Bacteriophages and microbial interactions
  • Nuclear Structure and Function
  • Microtubule and mitosis dynamics
  • Vagus Nerve Stimulation Research
  • Lipid Membrane Structure and Behavior

The University of Texas at Austin
2022-2025

Membrane curvature is essential to diverse cellular functions. While classically attributed structured domains, recent work illustrates that intrinsically disordered proteins are also potent drivers of membrane bending. Specifically, repulsive interactions among domains drive convex bending, while attractive concave creating membrane-bound, liquid-like condensates. How might contain both and affect curvature? Here, we examined chimeras combined interactions. When the domain was closer...

10.1126/sciadv.adg3485 article EN cc-by-nc Science Advances 2023-07-07

Remote and genetically targeted neuromodulation in the deep brain is important for understanding treatment of neurological diseases. Ultrasound-triggered mechanoluminescent technology offers a promising approach achieving remote modulation. However, its application has thus far been limited to shallow depths due challenges related low sonochemical reaction efficiency restricted photon yields. Here we report cascaded nanotransducer achieve efficient light emission upon ultrasound stimulation....

10.1021/acsnano.3c06577 article EN ACS Nano 2023-12-14

Clathrin-mediated endocytosis is an essential cellular pathway that enables signaling and recycling of transmembrane proteins lipids. During endocytosis, dozens cytosolic come together at the plasma membrane, assembling into a highly interconnected network drives endocytic vesicle biogenesis. Recently, multiple groups have reported early form flexible condensates, which provide platform for efficient assembly vesicles. Given importance this in dynamics how might cells regulate its stability?...

10.1093/pnasnexus/pgae342 article EN cc-by-nc PNAS Nexus 2024-08-21

Cell-type-specific activation of parvalbumin (PV)-expressing neurons in the external globus pallidus (GPe) through optogenetics has shown promise facilitating long-lasting movement dysfunction recovery mice with Parkinson's disease. However, its translational potential is hindered by adverse effects stemming from invasive implantation optical fibers into brain. In this study, we have developed a non-invasive approach, utilizing focused ultrasound-triggered mechanoluminescent nanotransducers...

10.1101/2025.01.03.631271 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2025-01-04

Clathrin-mediated endocytosis is an essential cellular pathway that enables signaling and recycling of transmembrane proteins lipids. During endocytosis, dozens cytosolic come together at the plasma membrane, assembling into a highly interconnected network drives endocytic vesicle biogenesis. Recently, multiple groups have reported early form flexible condensates, which provide platform for efficient assembly vesicles. Given importance this in dynamics how might cells regulate its stability?...

10.1101/2023.08.21.554139 preprint EN cc-by-nc bioRxiv (Cold Spring Harbor Laboratory) 2023-08-22

Abstract Membrane curvature is essential to diverse cellular functions. While classically attributed structured domains, recent work illustrates that intrinsically disordered proteins are also potent drivers of membrane bending. Specifically, repulsive interactions among domains drive convex bending, while attractive interactions, which lead liquid-like condensates, concave How might contain both and impact curvature? Here we examine chimeras combine interactions. When the domain was closer...

10.1101/2022.12.17.520884 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2022-12-17
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