Jay T. Groves

University of California, Berkeley

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John Kuriyan

Vanderbilt University

Jean K. Chung

Colorado State University

Kabir H. Biswas

Hamad bin Khalifa University

Kiera B. Wilhelm

University of California, Berkeley

Wan‐Chen Lin

Academia Sinica

William Y. C. Huang

Stanford University

Young Kwang Lee

San Diego State University

Jenny J. Lin

University of California, Berkeley

Steven Alvarez

University of California, Berkeley

Darren B. McAffee

University of California, Berkeley

Cooperative Institutions

University of California, Berkeley

210

Howard Hughes Medical Institute

115

Lawrence Berkeley National Laboratory

Berkeley College

University of California, San Francisco

QB3

Stanford University

National University of Singapore

Massachusetts Institute of Technology

University of California, Davis

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Fluorescence Imaging of Membrane Dynamics

Annual Review of Biomedical Engineering (2008)

Jay T. Groves R. Parthasarathy Martin B. Forstner

Imaging membrane dynamics is an important goal, motivated by the abundance of biochemical and biophysical events that are orchestrated at, or by, cellular membranes. The short length scales, fast timescales, and environmental requirements of membrane phenomena present challenges to imaging experiments. Several technical advances offer means to overcome these challenges, and we describe here three powerful techniques applicable to membrane imaging: total internal reflection fluorescence (TIRF) microscopy, fluorescence interference contrast (FLIC) microscopy, and fluorescence correlation spectroscopy (FCS). For each, we discuss the physics underpinning the approach, its practical implementation, and recent examples highlighting its achievements in exploring the membrane environment.

Fluorescence Correlation Spectroscopy

Fluorescence-lifetime imaging microscopy

10.1146/annurev.bioeng.10.061807.160431

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Citations (121)

Author response: Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation

Moitrayee Bhattacharyya Young Kwang Lee Serena Muratcioğlu Baiyu Qiu Priya Nyayapati

10.7554/elife.53670.sa2

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Protein Assembly on Membrane Surface alters the Dynamical Spectrum of Downstream Signaling Reactions

Biophysical Journal (2016)

William Y. C. Huang Qingrong Yan Wan‐Chen Lin Jean K. Chung Scott D. Hansen

Cell Signaling

Cell membrane

10.1016/j.bpj.2015.11.534

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TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation

Nature Immunology (2009)

Björn F. Lillemeier Manuel Mörtelmaier Martin B. Forstner Johannes B. Huppa Jay T. Groves

Cell membrane

Cell Signaling

10.1038/ni.1832

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Citations (613)

Building an affinity panel of synthetic polyclonal T-cell receptor ligands that mimic native peptide-MHC

Biophysical Journal (2023)

Anand Vissa Kiera B. Wilhelm Brittany Stinger Jay T. Groves

Polyclonal antibodies

10.1016/j.bpj.2022.11.2712

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The Formation of Lat Protein Condensates in Response to Single pMHC-TCR Binding Events

Biophysical Journal (2020)

Darren B. McAffee Shalini T. Low-Nam Jenny J. Lin Scott D. Hansen Steven Alvarez

Dwell time

Linker

10.1016/j.bpj.2019.11.1450

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Altered TCR Signaling from Geometrically Repatterned Immunological Synapses

Science (2005)

Kaspar Mossman Gabriele Campi Jay T. Groves Michael L. Dustin

The immunological synapse is a specialized cell-cell junction that is defined by large-scale spatial patterns of receptors and signaling molecules yet remains largely enigmatic in terms of formation and function. We used supported bilayer membranes and nanometer-scale structures fabricated onto the underlying substrate to impose geometric constraints on immunological synapse formation. Analysis of the resulting alternatively patterned synapses revealed a causal relation between the radial position of T cell receptors (TCRs) and signaling activity, with prolonged signaling from TCR microclusters that had been mechanically trapped in the peripheral regions of the synapse. These results are consistent with a model of the synapse in which spatial translocation of TCRs represents a direct mechanism of signal regulation.

Immunological synapse

Cell Signaling

10.1126/science.1119238

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Citations (534)

Competition for shared downstream signaling molecules establishes indirect negative feedback between EGFR and EphA2

Biophysical Journal (2022)

Dongmyung Oh Zhongwen Chen Kabir H. Biswas Funing Bai Hui Ting Ong

EPH receptor A2

Signalling

10.1016/j.bpj.2022.04.015

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Nanopore-mediated protein delivery enabling three-color single-molecule tracking in living cells

Proceedings of the National Academy of Sciences (2021)

Zhongwen Chen Yuhong Cao Chun‐Wei Lin Steven Alvarez Dongmyung Oh

Multicolor single-molecule tracking (SMT) provides a powerful tool to mechanistically probe molecular interactions in living cells. However, because of the limitations in the optical and chemical properties of currently available fluorophores and the multiprotein labeling strategies, intracellular multicolor SMT remains challenging for general research studies. Here, we introduce a practical method employing a nanopore-electroporation (NanoEP) technique to deliver multiple organic dye-labeled proteins into living cells for imaging. It can be easily expanded to three channels in commercial microscopes or be combined with other in situ labeling methods. Utilizing NanoEP, we demonstrate three-color SMT for both cytosolic and membrane proteins. Specifically, we simultaneously monitored single-molecule events downstream of EGFR signaling pathways in living cells. The results provide detailed resolution of the spatial localization and dynamics of Grb2 and SOS recruitment to activated EGFR along with the resultant Ras activation.

Nanopore

Tracking (education)

10.1073/pnas.2012229118

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A Nanocube Plasmonic Sensor for Molecular Binding on Membrane Surfaces

Nano Letters (2009)

William J. Galush Sarah A. Shelby Martin J. Mulvihill Andrea R. Tao Peidong Yang

Detection and characterization of molecular interactions on membrane surfaces is important to biological and pharmacological research. Here, silver nanocubes interfaced with glass-supported model membranes form a label-free sensor that measures protein binding to the membrane. The technique utilizes plasmon resonance scattering of nanocubes, which are chemically coupled to the membrane. In contrast to other plasmonic sensing techniques, this method features simple, solution-based device fabrication and readout. Static and dynamic protein/membrane binding are monitored and quantified.

Molecular binding

Characterization

10.1021/nl900513k

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Citations (117)