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Article ; Online: Regulation of T-cell receptor signaling by the actin cytoskeleton and poroelastic cytoplasm.

Beemiller, Peter / Krummel, Matthew F

2013 Volume 256, Issue 1, Page(s) 148–159

Abstract: The actin cytoskeleton plays essential roles in modulating T-cell activation. Most models of T-cell receptor (TCR) triggering signalosome assembly and immune synapse formation invoke actin-dependent mechanisms. As T cells are constitutively motile cells, ...

Abstract	The actin cytoskeleton plays essential roles in modulating T-cell activation. Most models of T-cell receptor (TCR) triggering signalosome assembly and immune synapse formation invoke actin-dependent mechanisms. As T cells are constitutively motile cells, TCR triggering and signaling occur against a cytoskeletal backdrop that is constantly remodeling. While the interplay between actin dynamics and TCR signaling have been the focus of research for many years, much of the work in T cells has considered actin largely for its 'scaffolding' function. We examine the roles of the actin cytoskeleton in TCR signaling and immune synapse formation with an emphasis on how poroelasticity, an ensemble feature of actin dynamics with the cytosol, relates to how T cells respond to stimulation.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Animals ; Cytoplasm/metabolism ; Humans ; Immunological Synapses/metabolism ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism
Chemical Substances	Receptors, Antigen, T-Cell
Language	English
Publishing date	2013-10-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/imr.12120
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Article ; Online: Mediation of T-cell activation by actin meshworks.

Beemiller, Peter / Krummel, Matthew F

Cold Spring Harbor perspectives in biology

2010 Volume 2, Issue 9, Page(s) a002444

Abstract: Although the actin cytoskeleton and T-cell receptor (TCR) signaling complexes are seemingly distinct molecular structures, they are tightly integrated in T cells. The signaling pathways initiated by TCRs binding to peptide MHC complexes are extensively ... ...

Abstract	Although the actin cytoskeleton and T-cell receptor (TCR) signaling complexes are seemingly distinct molecular structures, they are tightly integrated in T cells. The signaling pathways initiated by TCRs binding to peptide MHC complexes are extensively influenced by the actin cytoskeletal activities of the motile phase before TCR signaling, the signalosome scaffolding function of the cytoskeleton, and the translocation of signaling clusters that precedes the termination of signaling at these complexes. As these three successive phases constitute essentially all the steps consequent to immune synapse formation, it has become clear that the substantial physical forces and signaling interactions generated by the actin cytoskeleton dominate the signaling life cycle of TCR signalosomes. We discuss the contributions of the actin cytoskeleton to TCR signaling phases and model some remaining questions about how specific cytoskeletal factors regulate TCR signaling outcomes.
MeSH term(s)	Actins/immunology ; Cell Movement/immunology ; Cytoskeleton/immunology ; Histocompatibility Antigens/immunology ; Humans ; Lymphocyte Activation ; Receptors, Antigen, T-Cell/immunology ; Signal Transduction ; T-Lymphocytes/immunology
Chemical Substances	Actins ; Histocompatibility Antigens ; Receptors, Antigen, T-Cell
Language	English
Publishing date	2010-08-11
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1943-0264
ISSN (online)	1943-0264
DOI	10.1101/cshperspect.a002444
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Article ; Online: Distinct functions for HS1 in chemosensory versus adhesive signaling.

Beemiller, Peter / Krummel, Matthew F

Nature immunology

2008 Volume 9, Issue 8, Page(s) 833–834

MeSH term(s)	Blood Proteins/metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Signal Transduction/immunology ; Signal Transduction/physiology
Chemical Substances	Blood Proteins ; HCLS1 protein, human ; Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2008-08
Publishing country	United States
Document type	Comment ; News
ZDB-ID	2016987-5
ISSN	1529-2916 ; 1529-2908
ISSN (online)	1529-2916
ISSN	1529-2908
DOI	10.1038/ni0808-833
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Article ; Online: Integration of the movement of signaling microclusters with cellular motility in immunological synapses.

Beemiller, Peter / Jacobelli, Jordan / Krummel, Matthew F

Nature immunology

2012 Volume 13, Issue 8, Page(s) 787–795

Abstract: Immune synapses form between T cells and antigen-presenting cells (APCs). Increasing evidence suggests synapses must form flexibly to accommodate ongoing motility and displacement of the synapse. Here, time-lapse total internal reflection fluorescence ( ... ...

Abstract	Immune synapses form between T cells and antigen-presenting cells (APCs). Increasing evidence suggests synapses must form flexibly to accommodate ongoing motility and displacement of the synapse. Here, time-lapse total internal reflection fluorescence (TIRF) microscopy showed that signaling via the T cell antigen receptor (TCR) occurred during synapse translation. TCR microclusters in motile synapses did not flow directly into supramolecular activating complexes (SMACs) but were directed, independently of myosin II contractility, toward an F-actin-poor 'sink' region. Inward microcluster flow often followed collapse of the leading edge, which suggested that actin depolymerization regulated microcluster flow and the formation of SMACs. The coordination of TCR movement with the translocation of this 'sink' shows how T cells coordinate TCR signaling and microcluster flow in dynamic physiological synapses.
MeSH term(s)	Actins/metabolism ; Animals ; Antigen-Presenting Cells/immunology ; Antigen-Presenting Cells/metabolism ; Cell Communication ; Cell Membrane/immunology ; Cell Movement/immunology ; Cells, Cultured ; Immunological Synapses/immunology ; Lipid Bilayers/metabolism ; Lymphocyte Activation ; Mice ; Mice, Transgenic ; Microscopy, Fluorescence ; Myosin Type II/metabolism ; Receptors, Antigen, T-Cell/biosynthesis ; Receptors, Antigen, T-Cell/immunology ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism
Chemical Substances	Actins ; Lipid Bilayers ; Receptors, Antigen, T-Cell ; Myosin Type II (EC 3.6.1.-)
Language	English
Publishing date	2012-07-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2016987-5
ISSN	1529-2916 ; 1529-2908
ISSN (online)	1529-2916
ISSN	1529-2908
DOI	10.1038/ni.2364
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Article: Assessing and benchmarking multiphoton microscopes for biologists.

Corbin, Kaitlin / Pinkard, Henry / Peck, Sebastian / Beemiller, Peter / Krummel, Matthew F

Methods in cell biology

2014 Volume 123, Page(s) 135–151

Abstract: Multiphoton microscopy has become staple tool for tracking cells within tissues and organs due to superior depth of penetration, low excitation volumes, and reduced phototoxicity. Many factors, ranging from laser pulse width to relay optics to detectors ... ...

Abstract	Multiphoton microscopy has become staple tool for tracking cells within tissues and organs due to superior depth of penetration, low excitation volumes, and reduced phototoxicity. Many factors, ranging from laser pulse width to relay optics to detectors and electronics, contribute to the overall ability of these microscopes to excite and detect fluorescence deep within tissues. However, we have found that there are few standard ways already described in the literature to distinguish between microscopes or to benchmark existing microscopes to measure the overall quality and efficiency of these instruments. Here, we discuss some simple parameters and methods that can either be used within a multiphoton facility or by a prospective purchaser to benchmark performance. This can both assist in identifying decay in microscope performance and in choosing features of a scope that are suited to experimental needs.
MeSH term(s)	Benchmarking ; Cells, Cultured ; Green Fluorescent Proteins/biosynthesis ; Green Fluorescent Proteins/chemistry ; Humans ; Microscopy, Fluorescence, Multiphoton/instrumentation ; Microscopy, Fluorescence, Multiphoton/standards ; Signal-To-Noise Ratio ; Single-Cell Analysis/instrumentation ; Single-Cell Analysis/standards
Chemical Substances	Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2014-06-25
Publishing country	United States
Document type	Journal Article
ISSN	0091-679X
ISSN	0091-679X
DOI	10.1016/B978-0-12-420138-5.00008-2
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Article ; Online: Evolving immune circuits are generated by flexible, motile, and sequential immunological synapses.

Gérard, Audrey / Beemiller, Peter / Friedman, Rachel S / Jacobelli, Jordan / Krummel, Matthew F

Immunological reviews

2012 Volume 251, Issue 1, Page(s) 80–96

Abstract: The immune system is made up of a diverse collection of cells, each of which has distinct sets of triggers that elicit unique and overlapping responses. It is correctly described as a 'system' because its overall properties (e.g. 'tolerance', 'allergy') ... ...

Abstract	The immune system is made up of a diverse collection of cells, each of which has distinct sets of triggers that elicit unique and overlapping responses. It is correctly described as a 'system' because its overall properties (e.g. 'tolerance', 'allergy') emerge from multiple interactions of its components cells. To mobilize a response where needed, the majority of the cells of the system are obligatorily highly motile and so must communicate with one another over both time and space. Here, we discuss the flexibility of the primary immunological synapse (IS) with respect to motility. We then consider the primary IS as an initiating module that licenses 'immunological circuits': the latter consisting of two or more cell-cell synaptic interactions. We discuss how two or three component immunological circuits interact might with one another in sequence and how the timing, stoichiometry, milieu, and duration of assembly of immunological circuits are likely to be key determinants in the emergent outcome and thus the system-wide immune response. An evolving consideration of immunological circuits, with an emphasis on the cell-cell modules that complement T-antigen-presenting cell interaction, provides a fundamental starting point for systems analysis of the immune response.
MeSH term(s)	Animals ; Cell Communication/immunology ; Cell Movement/immunology ; Cellular Microenvironment/immunology ; Cytokinesis/immunology ; Humans ; Immune System ; Immunity, Cellular ; Immunological Synapses/immunology ; Receptor Cross-Talk ; Signal Transduction
Language	English
Publishing date	2012-12-06
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/imr.12021
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Article ; Online: A phosphatidylinositol-3-kinase-dependent signal transition regulates ARF1 and ARF6 during Fcgamma receptor-mediated phagocytosis.

Beemiller, Peter / Hoppe, Adam D / Swanson, Joel A

PLoS biology

2006 Volume 4, Issue 6, Page(s) e162

Abstract: Fcgamma receptor (FcgammaR)-mediated phagocytosis of IgG-coated particles is regulated by 3'-phosphoinositides (3'PIs) and several classes of small GTPases, including ARF6 from the ADP Ribosylation Factor subfamily. The insensitivity of phagocytosis to ... ...

Abstract	Fcgamma receptor (FcgammaR)-mediated phagocytosis of IgG-coated particles is regulated by 3'-phosphoinositides (3'PIs) and several classes of small GTPases, including ARF6 from the ADP Ribosylation Factor subfamily. The insensitivity of phagocytosis to brefeldin A (BFA), an inhibitor of certain ARF guanine nucleotide exchange factors (GEFs), previously indicated that ARF1 did not participate in phagocytosis. In this study, we show that ARF1 was activated during FcgammaR-mediated phagocytosis and that blocking normal ARF1 cycling inhibited phagosome closure. We examined the distributions and activation patterns of ARF6 and ARF1 during FcgammaR-mediated phagocytosis using fluorescence resonance energy transfer (FRET) stoichiometric microscopy of macrophages expressing CFP- or YFP-chimeras of ARF1, ARF6, and a GTP-ARF-binding protein domain. Both GTPases were activated by BFA-insensitive factors at sites of phagocytosis. ARF6 activation was restricted to the leading edge of the phagocytic cup, while ARF1 activation was delayed and delocalized over the phagosome. Phagocytic cups formed after inhibition of PI 3-kinase (PI-3K) contained persistently activated ARF6 and minimally activated ARF1. This indicates that a PI-3K-dependent signal transition defines the sequence of ARF GTPase activation during phagocytosis and that ARF6 and ARF1 coordinate different functions at the forming phagosome.
MeSH term(s)	ADP-Ribosylation Factor 1/analysis ; ADP-Ribosylation Factor 1/metabolism ; ADP-Ribosylation Factor 6 ; ADP-Ribosylation Factors/analysis ; ADP-Ribosylation Factors/metabolism ; Brefeldin A/pharmacology ; Cells, Cultured ; Enzyme Activation ; Fluorescence Resonance Energy Transfer ; Humans ; Macrophages/metabolism ; Mutation ; Phagocytosis/physiology ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositol 3-Kinases/physiology ; Phosphoinositide-3 Kinase Inhibitors ; Receptors, IgG/physiology ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
Chemical Substances	ADP-Ribosylation Factor 6 ; Phosphoinositide-3 Kinase Inhibitors ; Receptors, IgG ; Recombinant Fusion Proteins ; Brefeldin A (20350-15-6) ; ADP-Ribosylation Factor 1 (EC 3.6.5.2) ; ADP-Ribosylation Factors (EC 3.6.5.2) ; ARF6 protein, human (EC 3.6.5.2)
Language	English
Publishing date	2006-05-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.0040162
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Article ; Online: Visualizing dynamic microvillar search and stabilization during ligand detection by T cells.

Cai, En / Marchuk, Kyle / Beemiller, Peter / Beppler, Casey / Rubashkin, Matthew G / Weaver, Valerie M / Gérard, Audrey / Liu, Tsung-Li / Chen, Bi-Chang / Betzig, Eric / Bartumeus, Frederic / Krummel, Matthew F

Science (New York, N.Y.)

2017 Volume 356, Issue 6338

Abstract: During immune surveillance, T cells survey the surface of antigen-presenting cells. In searching for peptide-loaded major histocompatibility complexes (pMHCs), they must solve a classic trade-off between speed and sensitivity. It has long been supposed ... ...

Abstract	During immune surveillance, T cells survey the surface of antigen-presenting cells. In searching for peptide-loaded major histocompatibility complexes (pMHCs), they must solve a classic trade-off between speed and sensitivity. It has long been supposed that microvilli on T cells act as sensory organs to enable search, but their strategy has been unknown. We used lattice light-sheet and quantum dot-enabled synaptic contact mapping microscopy to show that anomalous diffusion and fractal organization of microvilli survey the majority of opposing surfaces within 1 minute. Individual dwell times were long enough to discriminate pMHC half-lives and T cell receptor (TCR) accumulation selectively stabilized microvilli. Stabilization was independent of tyrosine kinase signaling and the actin cytoskeleton, suggesting selection for avid TCR microclusters. This work defines the efficient cellular search process against which ligand detection takes place.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Animals ; Antigens/immunology ; Fractals ; Ligands ; Mice ; Microscopy/methods ; Microvilli/chemistry ; Microvilli/metabolism ; Quantum Dots ; Receptors, Antigen, T-Cell/metabolism ; T-Lymphocytes/cytology ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism
Chemical Substances	Antigens ; Ligands ; Receptors, Antigen, T-Cell
Language	English
Publishing date	2017-05-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.aal3118
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Article ; Online: Real-time analysis of T cell receptors in naive cells in vitro and in vivo reveals flexibility in synapse and signaling dynamics.

Friedman, Rachel S / Beemiller, Peter / Sorensen, Caitlin M / Jacobelli, Jordan / Krummel, Matthew F

The Journal of experimental medicine

2010 Volume 207, Issue 12, Page(s) 2733–2749

Abstract: The real-time dynamics of the T cell receptor (TCR) reflect antigen detection and T cell signaling, providing valuable insight into the evolving events of the immune response. Despite considerable advances in studying TCR dynamics in simplified systems ... ...

Abstract	The real-time dynamics of the T cell receptor (TCR) reflect antigen detection and T cell signaling, providing valuable insight into the evolving events of the immune response. Despite considerable advances in studying TCR dynamics in simplified systems in vitro, live imaging of subcellular signaling complexes expressed at physiological densities in intact tissues has been challenging. In this study, we generated a transgenic mouse with a TCR fused to green fluorescent protein to provide insight into the early signaling events of the immune response. To enable imaging of TCR dynamics in naive T cells in the lymph node, we enhanced signal detection of the fluorescent TCR fusion protein and used volumetric masking with a second fluorophore to mark the T cells expressing the fluorescent TCR. These in vivo analyses and parallel experiments in vitro show minimal and transient incorporation of TCRs into a stable central supramolecular activating cluster (cSMAC) structure but strong evidence for rapid, antigen-dependent TCR internalization that was not contingent on T cell motility arrest or cSMAC formation. Short-lived antigen-independent TCR clustering was also occasionally observed. These in vivo observations demonstrate that varied TCR trafficking and cell arrest dynamics occur during early T cell activation.
MeSH term(s)	Animals ; Dendritic Cells/physiology ; Fluorescence ; Immunological Synapses/physiology ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Receptors, Antigen, T-Cell/physiology ; Signal Transduction/physiology
Chemical Substances	Receptors, Antigen, T-Cell
Language	English
Publishing date	2010-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218343-2
ISSN	1540-9538 ; 0022-1007
ISSN (online)	1540-9538
ISSN	0022-1007
DOI	10.1084/jem.20091201
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Article ; Online: Secondary T cell-T cell synaptic interactions drive the differentiation of protective CD8+ T cells.

Gérard, Audrey / Khan, Omar / Beemiller, Peter / Oswald, Erin / Hu, Joyce / Matloubian, Mehrdad / Krummel, Matthew F

Nature immunology

2013 Volume 14, Issue 4, Page(s) 356–363

Abstract: Immunization results in the differentiation of CD8+ T cells, such that they acquire effector abilities and convert into a memory pool. Priming of T cells takes place via an immunological synapse formed with an antigen-presenting cell (APC). By disrupting ...

Abstract	Immunization results in the differentiation of CD8+ T cells, such that they acquire effector abilities and convert into a memory pool. Priming of T cells takes place via an immunological synapse formed with an antigen-presenting cell (APC). By disrupting synaptic stability at different times, we found that the differentiation of CD8+ T cells required cell interactions beyond those made with APCs. We identified a critical differentiation period that required interactions between primed T cells. We found that T cell-T cell synapses had a major role in the generation of protective CD8+ T cell memory. T cell-T cell synapses allowed T cells to polarize critical secretion of interferon-γ (IFN-γ) toward each other. Collective activation and homotypic clustering drove cytokine sharing and acted as regulatory stimuli for T cell differentiation.
MeSH term(s)	Animals ; Antigen-Presenting Cells/immunology ; Antigen-Presenting Cells/metabolism ; CD8-Positive T-Lymphocytes/cytology ; CD8-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/metabolism ; Cell Communication/immunology ; Cell Differentiation/immunology ; Cytokines/immunology ; Cytokines/metabolism ; Immunologic Memory ; Immunological Synapses ; Mice ; Mice, Knockout ; T-Lymphocyte Subsets/cytology ; T-Lymphocyte Subsets/immunology ; T-Lymphocyte Subsets/metabolism
Chemical Substances	Cytokines
Language	English
Publishing date	2013-03-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2016987-5
ISSN	1529-2916 ; 1529-2908
ISSN (online)	1529-2916
ISSN	1529-2908
DOI	10.1038/ni.2547
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