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Article ; Online: Author Correction: A rationally enhanced red fluorescent protein expands the utility of FRET biosensors.

Mo, Gary C H / Posner, Clara / Rodriguez, Erik A / Sun, Tengqian / Zhang, Jin

2024 Volume 15, Issue 1, Page(s) 771

Language	English
Publishing date	2024-01-26
Publishing country	England
Document type	Published Erratum
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-45330-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: DrFLINC Contextualizes Super-resolution Activity Imaging.

Lin, Wei / Mo, Gary C H / Mehta, Sohum / Zhang, Jin

Journal of the American Chemical Society

2021 Volume 143, Issue 37, Page(s) 14951–14955

Abstract: Super-resolution activity imaging maps the biochemical architecture of living cells yet currently overlooks the locations of collaborating regulators/effectors. Building on the fluorescence fluctuation increase by contact (FLINC) principle, here we ... ...

Abstract	Super-resolution activity imaging maps the biochemical architecture of living cells yet currently overlooks the locations of collaborating regulators/effectors. Building on the fluorescence fluctuation increase by contact (FLINC) principle, here we devise Dronpa-chromophore-removed FLINC (DrFLINC), where the nonfluorescent Dronpa can nevertheless enhance TagRFP-T fluorescence fluctuations. Exploiting DrFLINC, we develop a superior red label and a next-generation activity sensor for context-rich super-resolution biosensing.
MeSH term(s)	Fluorescence ; Fluorescent Dyes/chemistry ; Green Fluorescent Proteins/chemistry ; HeLa Cells ; Humans
Chemical Substances	Fluorescent Dyes ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2021-09-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.1c05530
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Article ; Online: Gasdermin D pores are dynamically regulated by local phosphoinositide circuitry.

Santa Cruz Garcia, Ana Beatriz / Schnur, Kevin P / Malik, Asrar B / Mo, Gary C H

Nature communications

2022 Volume 13, Issue 1, Page(s) 52

Abstract: Gasdermin D forms large, ~21 nm diameter pores in the plasma membrane to drive the cell death program pyroptosis. These pores are thought to be permanently open, and the resultant osmotic imbalance is thought to be highly damaging. Yet some cells ... ...

Abstract	Gasdermin D forms large, ~21 nm diameter pores in the plasma membrane to drive the cell death program pyroptosis. These pores are thought to be permanently open, and the resultant osmotic imbalance is thought to be highly damaging. Yet some cells mitigate and survive pore formation, suggesting an undiscovered layer of regulation over the function of these pores. However, no methods exist to directly reveal these mechanistic details. Here, we combine optogenetic tools, live cell fluorescence biosensing, and electrophysiology to demonstrate that gasdermin pores display phosphoinositide-dependent dynamics. We quantify repeated and fast opening-closing of these pores on the tens of seconds timescale, visualize the dynamic pore geometry, and identify the signaling that controls dynamic pore activity. The identification of this circuit allows pharmacological tuning of pyroptosis and control of inflammatory cytokine release by living cells.
MeSH term(s)	Animals ; Cell Death ; Cell Membrane/metabolism ; Cytokines/metabolism ; Electrophysiology ; Female ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Male ; Membrane Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Optogenetics ; Phosphate-Binding Proteins/genetics ; Phosphate-Binding Proteins/metabolism ; Phosphatidylinositols/metabolism ; Pyroptosis/physiology ; RAW 264.7 Cells
Chemical Substances	Cytokines ; GSDMD protein, human ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Phosphate-Binding Proteins ; Phosphatidylinositols
Language	English
Publishing date	2022-01-10
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-27692-9
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Article: DrFLINC Contextualizes Super-resolution Activity Imaging

Lin, Wei / Mo, Gary C.H. / Mehta, Sohum / Zhang, Jin

Journal of the American Chemical Society. 2021 Sept. 13, v. 143, no. 37

2021

Abstract	Super-resolution activity imaging maps the biochemical architecture of living cells yet currently overlooks the locations of collaborating regulators/effectors. Building on the fluorescence fluctuation increase by contact (FLINC) principle, here we devise Dronpa-chromophore-removed FLINC (DrFLINC), where the nonfluorescent Dronpa can nevertheless enhance TagRFP-T fluorescence fluctuations. Exploiting DrFLINC, we develop a superior red label and a next-generation activity sensor for context-rich super-resolution biosensing.
Keywords	Americans ; fluorescence ; image analysis ; journals
Language	English
Dates of publication	2021-0913
Size	p. 14951-14955.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.1c05530
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Article ; Online: A rationally enhanced red fluorescent protein expands the utility of FRET biosensors.

Mo, Gary C H / Posner, Clara / Rodriguez, Erik A / Sun, Tengqian / Zhang, Jin

Nature communications

2020 Volume 11, Issue 1, Page(s) 1848

Abstract: Genetically encoded Förster Resonance Energy Transfer (FRET)-based biosensors are powerful tools to illuminate spatiotemporal regulation of cell signaling in living cells, but the utility of the red spectrum for biosensing was limited due to a lack of ... ...

Abstract	Genetically encoded Förster Resonance Energy Transfer (FRET)-based biosensors are powerful tools to illuminate spatiotemporal regulation of cell signaling in living cells, but the utility of the red spectrum for biosensing was limited due to a lack of bright and stable red fluorescent proteins. Here, we rationally improve the photophysical characteristics of the coral-derived fluorescent protein TagRFP-T. We show that a new single-residue mutant, super-TagRFP (stagRFP) has nearly twice the molecular brightness of TagRFP-T and negligible photoactivation. stagRFP facilitates significant improvements on multiple green-red biosensors as a FRET acceptor and is an efficient FRET donor that supports red/far-red FRET biosensing. Capitalizing on the ability of stagRFP to couple with multiple FRET partners, we develop a novel multiplex method to examine the confluence of signaling activities from three kinases simultaneously in single living cells, providing evidence for a role of Src family kinases in regulating growth factor induced Akt and ERK activities.
MeSH term(s)	Fluorescence Resonance Energy Transfer ; Humans ; Luminescent Proteins/chemistry ; Mutagenesis/genetics ; Mutagenesis/physiology ; Signal Transduction/genetics ; Signal Transduction/physiology ; Red Fluorescent Protein
Chemical Substances	Luminescent Proteins
Language	English
Publishing date	2020-04-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-020-15687-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Structural templating of J-aggregates: Visualizing bis(monoacylglycero)phosphate domains in live cells.

Mo, Gary C H / Yip, Christopher M

Biochimica et biophysica acta. Proteins and proteomics

2017 Volume 1865, Issue 11 Pt B, Page(s) 1687–1695

Abstract: Identifying the key structural and dynamical determinants that drive the association of biomolecules, whether in solution, or perhaps more importantly in a membrane environment, has critical implications for our understanding of cellular dynamics, ... ...

Abstract	Identifying the key structural and dynamical determinants that drive the association of biomolecules, whether in solution, or perhaps more importantly in a membrane environment, has critical implications for our understanding of cellular dynamics, processes, and signaling. With recent advances in high-resolution imaging techniques, from the development of new molecular labels to technical advances in imaging methodologies and platforms, researchers are now reaping the benefits of being able to directly characterize and quantify local dynamics, structures, and conformations in live cells and tissues. These capabilities are providing unique insights into association stoichiometries, interactions, and structures on sub-micron length scales. We previously examined the role of lipid headgroup chemistry and phase state in guiding the formation of pseudoisocyanine (PIC) dye J-aggregates on supported planar bilayers [Langmuir, 25, 10719]. We describe here how these same J-aggregates can report on the in situ formation of organellar membrane domains in live cells. Live cell hyperspectral confocal microscopy using GFP-conjugated GTPase markers of early (Rab5) and late (Rab7) endosomes revealed that the PIC J-aggregates were confined to domains on either the limiting membrane or intralumenal vesicles (ILV) of late endosomes, known to be enriched in the anionic lipid bis(monoacylglycero)phosphate (BMP). Correlated confocal fluorescence - atomic force microscopy performed on endosomal membrane-mimetic supported planar lipid bilayers confirmed BMP-specific templating of the PIC J-aggregates. These data provide strong evidence for the formation of BMP-rich lipid domains during multivesicular body formation and portend the application of structured dye aggregates as markers of cellular membrane domain structure, size, and formation.
MeSH term(s)	Animals ; CHO Cells ; Cricetulus ; Endosomes/metabolism ; Endosomes/ultrastructure ; Glycerophosphates/metabolism ; Hep G2 Cells ; Humans ; Intracellular Membranes/metabolism ; Intracellular Membranes/ultrastructure ; Membrane Microdomains/metabolism ; Membrane Microdomains/ultrastructure ; Mice ; Microscopy, Atomic Force ; Microscopy, Confocal ; Monoglycerides/metabolism ; NIH 3T3 Cells ; rab GTP-Binding Proteins/metabolism ; rab5 GTP-Binding Proteins/metabolism
Chemical Substances	Glycerophosphates ; Monoglycerides ; rab7 protein (152989-05-4) ; RAB5C protein, human (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2) ; rab5 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2017-08-24
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 1570-9639 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	1570-9639 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2017.07.019
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Article: Structural templating of J-aggregates: Visualizing bis(monoacylglycero)phosphate domains in live cells

Mo, Gary C.H / Christopher M. Yip

Biochimica et biophysica acta. 2017 Nov., v. 1865, no. 11

2017

Abstract	Identifying the key structural and dynamical determinants that drive the association of biomolecules, whether in solution, or perhaps more importantly in a membrane environment, has critical implications for our understanding of cellular dynamics, processes, and signaling. With recent advances in high-resolution imaging techniques, from the development of new molecular labels to technical advances in imaging methodologies and platforms, researchers are now reaping the benefits of being able to directly characterize and quantify local dynamics, structures, and conformations in live cells and tissues. These capabilities are providing unique insights into association stoichiometries, interactions, and structures on sub-micron length scales. We previously examined the role of lipid headgroup chemistry and phase state in guiding the formation of pseudoisocyanine (PIC) dye J-aggregates on supported planar bilayers [Langmuir, 25, 10719]. We describe here how these same J-aggregates can report on the in situ formation of organellar membrane domains in live cells. Live cell hyperspectral confocal microscopy using GFP-conjugated GTPase markers of early (Rab5) and late (Rab7) endosomes revealed that the PIC J-aggregates were confined to domains on either the limiting membrane or intralumenal vesicles (ILV) of late endosomes, known to be enriched in the anionic lipid bis(monoacylglycero)phosphate (BMP). Correlated confocal fluorescence - atomic force microscopy performed on endosomal membrane-mimetic supported planar lipid bilayers confirmed BMP-specific templating of the PIC J-aggregates. These data provide strong evidence for the formation of BMP-rich lipid domains during multivesicular body formation and portend the application of structured dye aggregates as markers of cellular membrane domain structure, size, and formation.
Keywords	atomic force microscopy ; confocal microscopy ; endosomes ; fluorescence ; guanosinetriphosphatase ; image analysis ; lipid bilayers ; lipids ; phosphates ; proteins
Language	English
Dates of publication	2017-11
Size	p. 1687-1695.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2918798-9
ISSN	1878-1454 ; 1570-9639
ISSN (online)	1878-1454
ISSN	1570-9639
DOI	10.1016/j.bbapap.2017.07.019
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Article ; Online: Observing the Assembly of Protein Complexes in Living Eukaryotic Cells in Super-Resolution Using refSOFI.

Hertel, Fabian / Mo, Gary C H / Dedecker, Peter / Zhang, Jin

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1764, Page(s) 267–277

Abstract: Few approaches are currently available that allow the detection of protein-protein interactions (PPIs) in super-resolution, and the observation of the assembly of protein complexes in living cells has been particularly challenging. We developed ... ...

Abstract	Few approaches are currently available that allow the detection of protein-protein interactions (PPIs) in super-resolution, and the observation of the assembly of protein complexes in living cells has been particularly challenging. We developed reconstituted fluorescence-based stochastic optical fluctuation imaging (refSOFI), which is based on bimolecular fluorescence complementation (BiFC) and SOFI, allowing us to detect protein complex assembly 30 min after the induction of complex formation. Here we describe how to use refSOFI to map the assembly of two proteins of interest into a complex within living cells at super-resolution.
MeSH term(s)	Fluorescence ; HeLa Cells ; Humans ; Microscopy, Fluorescence/methods ; Neoplasm Proteins/metabolism ; ORAI1 Protein/metabolism ; Optical Imaging/methods ; Protein Interaction Domains and Motifs ; Stromal Interaction Molecule 1/metabolism
Chemical Substances	Neoplasm Proteins ; ORAI1 Protein ; ORAI1 protein, human ; STIM1 protein, human ; Stromal Interaction Molecule 1
Language	English
Publishing date	2018-01-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7759-8_16
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Article ; Online: Lifespan based pharmacokinetic-pharmacodynamic model of tumor growth inhibition by anticancer therapeutics.

Mo, Gary / Gibbons, Frank / Schroeder, Patricia / Krzyzanski, Wojciech

PloS one

2014 Volume 9, Issue 10, Page(s) e109747

Abstract: Accurate prediction of tumor growth is critical in modeling the effects of anti-tumor agents. Popular models of tumor growth inhibition (TGI) generally offer empirical description of tumor growth. We propose a lifespan-based tumor growth inhibition (LS ... ...

Abstract	Accurate prediction of tumor growth is critical in modeling the effects of anti-tumor agents. Popular models of tumor growth inhibition (TGI) generally offer empirical description of tumor growth. We propose a lifespan-based tumor growth inhibition (LS TGI) model that describes tumor growth in a xenograft mouse model, on the basis of cellular lifespan T. At the end of the lifespan, cells divide, and to account for tumor burden on growth, we introduce a cell division efficiency function that is negatively affected by tumor size. The LS TGI model capability to describe dynamic growth characteristics is similar to many empirical TGI models. Our model describes anti-cancer drug effect as a dose-dependent shift of proliferating tumor cells into a non-proliferating population that die after an altered lifespan TA. Sensitivity analysis indicated that all model parameters are identifiable. The model was validated through case studies of xenograft mouse tumor growth. Data from paclitaxel mediated tumor inhibition was well described by the LS TGI model, and model parameters were estimated with high precision. A study involving a protein casein kinase 2 inhibitor, AZ968, contained tumor growth data that only exhibited linear growth kinetics. The LS TGI model accurately described the linear growth data and estimated the potency of AZ968 that was very similar to the estimate from an established TGI model. In the case study of AZD1208, a pan-Pim inhibitor, the doubling time was not estimable from the control data. By fixing the parameter to the reported in vitro value of the tumor cell doubling time, the model was still able to fit the data well and estimated the remaining parameters with high precision. We have developed a mechanistic model that describes tumor growth based on cell division and has the flexibility to describe tumor data with diverse growth kinetics.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacokinetics ; Antineoplastic Agents/therapeutic use ; Antineoplastic Agents/toxicity ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; Dose-Response Relationship, Drug ; Female ; Half-Life ; Humans ; Mice ; Models, Biological ; Neoplasms/drug therapy ; Paclitaxel/pharmacokinetics ; Paclitaxel/therapeutic use ; Paclitaxel/toxicity ; Protein Kinase Inhibitors/pharmacokinetics ; Protein Kinase Inhibitors/therapeutic use ; Protein Kinase Inhibitors/toxicity ; Transplantation, Heterologous
Chemical Substances	Antineoplastic Agents ; Protein Kinase Inhibitors ; Paclitaxel (P88XT4IS4D)
Language	English
Publishing date	2014-10-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0109747
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Article ; Online: Solving delay differential equations in S-ADAPT by method of steps.

Bauer, Robert J / Mo, Gary / Krzyzanski, Wojciech

Computer methods and programs in biomedicine

2013 Volume 111, Issue 3, Page(s) 715–734

Abstract: S-ADAPT is a version of the ADAPT program that contains additional simulation and optimization abilities such as parametric population analysis. S-ADAPT utilizes LSODA to solve ordinary differential equations (ODEs), an algorithm designed for large ... ...

Abstract	S-ADAPT is a version of the ADAPT program that contains additional simulation and optimization abilities such as parametric population analysis. S-ADAPT utilizes LSODA to solve ordinary differential equations (ODEs), an algorithm designed for large dimension non-stiff and stiff problems. However, S-ADAPT does not have a solver for delay differential equations (DDEs). Our objective was to implement in S-ADAPT a DDE solver using the methods of steps. The method of steps allows one to solve virtually any DDE system by transforming it to an ODE system. The solver was validated for scalar linear DDEs with one delay and bolus and infusion inputs for which explicit analytic solutions were derived. Solutions of nonlinear DDE problems coded in S-ADAPT were validated by comparing them with ones obtained by the MATLAB DDE solver dde23. The estimation of parameters was tested on the MATLB simulated population pharmacodynamics data. The comparison of S-ADAPT generated solutions for DDE problems with the explicit solutions as well as MATLAB produced solutions which agreed to at least 7 significant digits. The population parameter estimates from using importance sampling expectation-maximization in S-ADAPT agreed with ones used to generate the data.
MeSH term(s)	Algorithms ; Computer Simulation ; Pharmacokinetics ; Systems Biology
Language	English
Publishing date	2013-09
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	632564-6
ISSN	1872-7565 ; 0169-2607
ISSN (online)	1872-7565
ISSN	0169-2607
DOI	10.1016/j.cmpb.2013.05.026
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