Dr Qian Peter SU is now an Emerging Leadership 1 Fellow (2020-25) of Australia National Health and Medical Research Council (NHMRC) and Postdoctoral Fellow (2020-22, co-fund) of National Heart Foundation. He is a Lecturer and the Group Leader of the Laboratory of Quantitative Imaging At Nanoscale with SUper-resolution (QIAN SU LAB) in the School of Biomedical Engineering at University of Technology Sydney. He is also part-time visiting scientists at Heart Research Institute and Centenary Institute at the University of Sydney.
His research focuses on establishing an “Imaging Profiling Platform for Cardiovascular Disease” supported by the Volumetric Imaging Facility (VIF), of which Peter is the facility manager and key operator. In 2017, Dr SU received his PhD in Biophysics supervised by Profs Xiaoliang Sunney XIE and Yujie SUN from Biodynamic Optical Imaging Centre (BIOPIC) in Peking University (PKU) with the honour of “Outstanding Graduate Student of the Beijing City”. In 2012, Dr SU took an oversea exchange scholarship and received mentorship on instrumentation of super-resolution microscopy in Profs Xiaoliang Sunney XIE and Xiaowei ZHUANG’s labs at Harvard University. He received his B.Eng. in Bio-Engineering supervised by Prof Linhong DENG in 2011 from College of Bioengineering, Chongqing University.
- Young Biophysicist Award, Australian Society for Biophysics (ASB), Canberra, Australia (2019)
- Rising Star Finalist, Sydney 2018 Cardiovascular Symposium, USYD, Australia (2018)
- Early Career Scientist Speaker Award, Asian Biophysics Association Symposium/ASB, Australia (2018)
- Poster Award, 4th Charles Perkins Centre (CPC) EMCR symposium, USYD, Australia (2018)
- EMCR Catalyst Award Recipients in Biomedical Engineering, University of Sydney, Australia (2018)
- Outstanding Graduate Student of the Beijing City, Beijing Education Bureau, China (2017)
- National Scholarship for (under)graduate student, Ministry of Education, China (2008,09,10,11,16)
- Second Prize, Poster Section, Cold Spring Harbor Asia Conference, Jiangsu, China (2013)
- Tanglixin Scholarship, Chongqing University/Peking University, Education Bureau, China (2009-2017)
Dr SU serves as the external peer reviewer for international journals, including JACS, Chemical Science, Analytical Chemistry, Journal of Biophotonics, Nano Letters, and Scientific Reports etc.
He is society members of NSW Cardiovascular Research Network (CVRN), Australia and New Zealand Society for Cell and Developmental Biology (ANZSCDB, NSW committee member), Australian Cardiovascular Alliance (ACvA Bioengineering flagship), Australia Society for Biophysics (ASB), Australia Nanotechnology Network (ANN), Australia Centre for Microscopy and Microanalysis (ACMM) and American Association for the Advancement of Science (AAAS).
Peter is actively involved in the organising committee for academic activities for Australian Societies. He is currently an organising committee member for International Mechanobiology Symposium 2020 (1-4 Nov 2020, chaired by Prof Boris MARTINAC, http://ausmb.org/index.html), responsible for the early career researcher (ECR) session and the funding raising. He served as an organising committee member for the ANZSCDB New South Wales 2019 Meeting held on 12th June 2019.
Can supervise: YES
Dr Q.Peter SU’s research bridges applied biomedical engineering with fundamental sciences. It brings new insights to mechanistic questions addressed at single-molecule level by advanced microscopy and acquired with high spatiotemporal resolution. He has developed state-of-art biophysical nanotools, including single-molecule in vitro reconstitution assays and super-resolution microscopy to visualise the precise structures and pinpoint the molecular mechanisms during important biological processes, including:
i) Deciphering the molecular interaction dynamics (termed “interactome”) for the mechanosensor integrin αIIbβ3 during human platelet decision-making process, under clinical trialed drug treatment for cardiovascular diseases, including thrombosis and type 2 diabetes (Nature Materials 2019, Nature Comm. 2018);
ii) Developing advanced single-molecule imaging, tracking and manipulation techniques to study motor proteins and cytoskeleton driven intracellular bio-membrane dynamics and the underlying molecular mechanisms, especially using in vitro re-constitution systems (Nature Cell Biology 2015, Developmental Cell 2016, Cell Research 2015a; Nat. Comm. 2017; PNAS 2016);
iii) Developing and applying cutting-edge super-resolution imaging systems and algorithms to resolve the precise structures of subcellular organelles, to map the spatial-temporal distribution of important proteins, to reveal the hierarchical chromatin structures as well as structure-mediated replication and transcription mechanisms in mammalian cell nucleus and bacterial chromatin (Nat. Comm 2014; Cell Research 2015b).
Zheng, P, Su, QP, Jin, D, Yu, Y & Huang, XF 2020, 'Prevention of Neurite Spine Loss Induced by Dopamine D2 Receptor Overactivation in Striatal Neurons', Frontiers in Neuroscience, vol. 14.View/Download from: Publisher's site
© Copyright © 2020 Zheng, Su, Jin, Yu and Huang. Psychosis has been considered a disorder of impaired neuronal connectivity. Evidence for excessive formation of dopamine D2 receptor (D2R) – disrupted in schizophrenia 1 (DISC1) complexes has led to a new perspective on molecular mechanisms involved in psychotic symptoms. Here, we investigated how excessive D2R–DISC1 complex formation induced by D2R agonist quinpirole affects neurite growth and dendritic spines in striatal neurons. Fluorescence resonance energy transfer (FRET), stochastic optical reconstruction microscopy (STORM), and cell penetrating-peptide delivery were used to study the cultured striatal neurons from mouse pups. Using these striatal neurons, our study showed that: (1) D2R interacted with DISC1 in dendritic spines, neurites and soma of cultured striatal neurons; (2) D2R and DISC1 complex accumulated in clusters in dendritic spines of striatal neurons and the number of the complex were reduced after application of TAT-D2pep; (3) uncoupling D2R–DISC1 complexes by TAT-D2pep protected neuronal morphology and dendritic spines; and (4) TAT-D2pep prevented neurite and dendritic spine loss, which was associated with restoration of expression levels of synaptophysin and PSD-95. In addition, we found that Neuropeptide Y (NPY) and GSK3β were involved in the protective effects of TAT-D2pep on the neurite spines of striatal spiny projection neurons. Thus, our results may offer a new strategy for precisely treating neurite spine deficits associated with schizophrenia.
Hao, H, Niu, J, Xue, B, Su, QP, Liu, M, Yang, J, Qin, J, Zhao, S, Wu, C & Sun, Y 2020, 'Golgi-associated microtubules are fast cargo tracks and required for persistent cell migration', EMBO REPORTS, vol. 21, no. 3.View/Download from: Publisher's site
Su, QP, Zhao, ZW, Meng, L, Ding, M, Zhang, W, Li, Y, Liu, M, Li, R, Gao, YQ, Xie, XS & Sun, Y 2020, 'Superresolution imaging reveals spatiotemporal propagation of human replication foci mediated by CTCF-organized chromatin structures', Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 26, pp. 15036-15046.View/Download from: Publisher's site
Mammalian DNA replication is initiated at numerous replication origins, which are clustered into thousands of replication domains (RDs) across the genome. However, it remains unclear whether the replication origins within each RD are activated stochastically or preferentially near certain chromatin features. To understand how DNA replication in single human cells is regulated at the sub-RD level, we directly visualized and quantitatively characterized the spatiotemporal organization, morphology, and in situ epigenetic signatures of individual replication foci (RFi) across S-phase at superresolution using stochastic optical reconstruction microscopy. Importantly, we revealed a hierarchical radial pattern of RFi propagation dynamics that reverses directionality from early to late S-phase and is diminished upon caffeine treatment or CTCF knockdown. Together with simulation and bioinformatic analyses, our findings point to a "CTCF-organized REplication Propagation" (CoREP) model, which suggests a nonrandom selection mechanism for replication activation at the sub-RD level during early S-phase, mediated by CTCF-organized chromatin structures. Collectively, these findings offer critical insights into the key involvement of local epigenetic environment in coordinating DNA replication across the genome and have broad implications for our conceptualization of the role of multiscale chromatin architecture in regulating diverse cell nuclear dynamics in space and time.
Liu, B, Chen, C, Di, X, Liao, J, Wen, S, Su, QP, Shan, X, Xu, Z-Q, Ju, LA, Mi, C, Wang, F & Jin, D 2020, 'Upconversion Nonlinear Structured Illumination Microscopy', NANO LETTERS, vol. 20, no. 7, pp. 4775-4781.View/Download from: Publisher's site
Chen, Y, Ju, LA, Zhou, F, Liao, J, Xue, L, Su, QP, Jin, D, Yuan, Y, Lu, H, Jackson, SP & Zhu, C 2019, 'An integrin αIIbβ3 intermediate affinity state mediates biomechanical platelet aggregation.', Nature materials, vol. 18, no. 7, pp. 760-769.View/Download from: Publisher's site
Integrins are membrane receptors that mediate cell adhesion and mechanosensing. The structure-function relationship of integrins remains incompletely understood, despite the extensive studies carried out because of its importance to basic cell biology and translational medicine. Using a fluorescence dual biomembrane force probe, microfluidics and cone-and-plate rheometry, we applied precisely controlled mechanical stimulations to platelets and identified an intermediate state of integrin αIIbβ3 that is characterized by an ectodomain conformation, ligand affinity and bond lifetimes that are all intermediate between the well-known inactive and active states. This intermediate state is induced by ligand engagement of glycoprotein (GP) Ibα via a mechanosignalling pathway and potentiates the outside-in mechanosignalling of αIIbβ3 for further transition to the active state during integrin mechanical affinity maturation. Our work reveals distinct αIIbβ3 state transitions in response to biomechanical and biochemical stimuli, and identifies a role for the αIIbβ3 intermediate state in promoting biomechanical platelet aggregation.
© Springer Science+Business Media, LLC, part of Springer Nature 2019. Autophagic lysosome reformation (ALR) is the terminal step of autophagy. ALR functions to recycle lysosomal membranes and maintain lysosome homeostasis. Maintaining a functional lysosome pool is critical for generating autolysosomes, in which cellular components are degraded and turned over during autophagy. This unit describes methods to visualize ALR in cells. In addition, this unit provides detailed protocols to establish in vitro systems which can be used to reconstitute ALR as well as to reconstitute mitochondrial tubulation/network formation, another process that is driven by motor proteins.
Intracellular membrane dynamics, especially the nano-tube formation, plays important roles in vesicle transportation and organelle biogenesis. Regarding the regulation mechanisms, it is well known that during the nano-tube formation, motor proteins act as the driven force moving along the cytoskeleton, lipid composition and its associated proteins serve as the linkers and key mediators, and the vesicle sizes play as one of the important regulators. In this review, we summarized the in vitro reconstitution assay method, which has been applied to reconstitute the nano-tube dynamics during autophagic lysosomal regeneration (ALR) and the morphology dynamics during mitochondria network formation (MNF) in a mimic and pure in vitro system. Combined with the single-molecule microscopy, the advantage of the in vitro reconstitution system is to study the key questions at a single-molecule or single-vesicle level with precisely tuned parameters and conditions, such as the motor mutation, ion concentration, lipid component, ATP/GTP concentration, and even in vitro protein knockout, which cannot easily be achieved by in vivo or intracellular studies.
Su, QP, Zhao, ZW, Meng, L, Ding, M, Zhang, W, Li, Y, Liu, M, Li, R, Gao, Y-Q, Xie, XS & Sun, Y 2019, 'CTCF-mediated Chromatin Structures Dictate the Spatio-temporal Propagation of Replication Foci: Supplementary Materials'.View/Download from: Publisher's site
Mammalian DNA replication is initiated at numerous replication origins, which are clustered into thousands of replication domains (RDs) across the genome. However, it remains unclear whether the replication origins within each RD are activated stochastically. To understand how replication is regulated at the sub-RD level, we directly visualized the spatio-temporal organization, morphology, and in situ epigenetic signatures of individual replication foci (RFi) across S-phase using super-resolution stochastic optical reconstruction microscopy (STORM). Importantly, we revealed a hierarchical radial pattern of RFi propagation that reverses its directionality from early to late S-phase, and is diminished upon caffeine treatment or CTCF knockdown. Together with simulation and bioinformatic analyses, our findings point to a "CTCF-organized REplication Propagation" (CoREP) model. The CoREP model suggests a non-random selection mechanism for replication activation mediated by CTCF at the sub-RD level, as well as the critical involvement of local chromatin environment in regulating replication in space and time.
Chen, C, Wang, F, Wen, S, Su, QP, Wu, MCL, Liu, Y, Wang, B, Li, D, Shan, X, Kianinia, M, Aharonovich, I, Toth, M, Jackson, SP, Xi, P & Jin, D 2018, 'Multi-photon near-infrared emission saturation nanoscopy using upconversion nanoparticles.', Nature communications, vol. 9, no. 1.View/Download from: Publisher's site
Multiphoton fluorescence microscopy (MPM), using near infrared excitation light, provides increased penetration depth, decreased detection background, and reduced phototoxicity. Using stimulated emission depletion (STED) approach, MPM can bypass the diffraction limitation, but it requires both spatial alignment and temporal synchronization of high power (femtosecond) lasers, which is limited by the inefficiency of the probes. Here, we report that upconversion nanoparticles (UCNPs) can unlock a new mode of near-infrared emission saturation (NIRES) nanoscopy for deep tissue super-resolution imaging with excitation intensity several orders of magnitude lower than that required by conventional MPM dyes. Using a doughnut beam excitation from a 980 nm diode laser and detecting at 800 nm, we achieve a resolution of sub 50 nm, 1/20th of the excitation wavelength, in imaging of single UCNP through 93 μm thick liver tissue. This method offers a simple solution for deep tissue super resolution imaging and single molecule tracking.
Chen, Y, Su, QP, Sun, Y & Yu, L 2018, 'Visualizing Autophagic Lysosome Reformation in Cells Using In Vitro Reconstitution Systems.', Current protocols in cell biology, vol. 78, no. 1, pp. 11.24.1-11.24.15.View/Download from: Publisher's site
Autophagy is a lysosome-based degradation pathway. Autophagic lysosome reformation (ALR) is a lysosomal membrane recycling process that marks the terminal step of autophagy. During ALR, LAMP1-positive tubules, named reformation tubules, are extruded from autolysosomes, and nascent lysosomes are generated from these tubules. By combining proteomic analysis of purified autolysosomes and RNA interference screening of identified candidates, we systematically elucidated the ALR pathway at the molecular level. Based on the key components clathrin, PtdIns(4,5)P2 , and the motor protein KIF5B, among others, we reconstituted this process in vitro. This unit describes a detailed method for visualizing ALR in cells during the autophagy process. This unit also present a protocol for reconstituting the ALR tubular protrusion and elongation process in vitro and three methods for preparing materials for in vitro reconstitution: (1) autolysosome purification from cultured cells, (2) liposome preparation, and (3) KIF5B purification and quality testing. © 2018 by John Wiley & Sons, Inc.
© 2018, International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature. The focus of the cell biology field is now shifting from characterizing cellular activities to organelle and molecular behaviors. This process accompanies the development of new biophysical visualization techniques that offer high spatial and temporal resolutions with ultra-sensitivity and low cell toxicity. They allow the biology research community to observe dynamic behaviors from scales of single molecules, organelles, cells to organoids, and even live animal tissues. In this review, we summarize these biophysical techniques into two major classes: the mechanical nanotools like dynamic force spectroscopy (DFS) and the optical nanotools like single-molecule and super-resolution microscopy. We also discuss their applications in elucidating molecular dynamics and functionally mapping of interactions between inter-cellular networks and intra-cellular components, which is key to understanding cellular processes such as adhesion, trafficking, inheritance, and division.
Ren, W, Wen, S, Tawfik, SA, Su, QP, Lin, G, Ju, LA, Ford, MJ, Ghodke, H, van Oijen, AM & Jin, D 2018, 'Anisotropic functionalization of upconversion nanoparticles.', Chemical science, vol. 9, no. 18, pp. 4352-4358.View/Download from: Publisher's site
Despite significant advances toward accurate tuning of the size and shape of colloidal nanoparticles, the precise control of the surface chemistry thereof remains a grand challenge. It is desirable to conjugate functional bio-molecules onto the selected facets of nanoparticles owing to the versatile capabilities rendered by the molecules. We report here facet-selective conjugation of DNA molecules onto upconversion nanoparticles via ligand competition reaction. Different binding strengths of phosphodiester bonds and phosphate groups on DNA and the surfactant molecules allow one to create heterogeneous bio-chemistry surface for upconversion nanoparticles. The tailored surface properties lead to the formation of distinct self-assembly structures. Our findings provide insight into the interactions between biomolecules and nanoparticles, unveiling the potential of using nanoparticles as fundamental building blocks for creating self-assembled nano-architectures.
Guan, R, Zhang, L, Su, QP, Mickolajczyk, KJ, Chen, G-Y, Hancock, WO, Sun, Y, Zhao, Y & Chen, Z 2017, 'Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin', NATURE COMMUNICATIONS, vol. 8.View/Download from: Publisher's site
Hao, H, Su, Q, Zhao, S & Sun, Y 2017, 'Golgi Microtubules are Hyper-Acetylated and Participate in Fast Cargo Trafficking', Biophysical Journal, vol. 112, no. 3, pp. 238a-238a.View/Download from: Publisher's site
Su, QP, Du, W, Ji, Q, Xue, B, Jiang, D, Zhu, Y, Ren, H, Zhang, C, Lou, J, Yu, L & Sun, Y 2017, 'Corrigendum: Vesicle Size Regulates Nanotube Formation in the Cell', Scientific reports, vol. 7, p. 40108.View/Download from: Publisher's site
Du, W, Su, QP, Chen, Y, Zhu, Y, Jiang, D, Rong, Y, Zhang, S, Zhang, Y, Ren, H, Zhang, C, Wang, X, Gao, N, Wang, Y, Sun, L, Sun, Y & Yu, L 2016, 'Kinesin 1 Drives Autolysosome Tubulation', DEVELOPMENTAL CELL, vol. 37, no. 4, pp. 326-336.View/Download from: Publisher's site
Shen, M, Zhang, N, Zheng, S, Zhang, W-B, Zhang, H-M, Lu, Z, Su, QP, Sun, Y, Ye, K & Li, X-D 2016, 'Calmodulin in complex with the first IQ motif of myosin-5a functions as an intact calcium sensor', PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 113, no. 40, pp. E5812-E5820.View/Download from: Publisher's site
Su, QP, Du, W, Ji, Q, Xue, B, Jiang, D, Zhu, Y, Lou, J, Yu, L & Sun, Y 2016, 'Vesicle Size Regulates Nanotube Formation in the Cell', Scientific Reports, vol. 6, pp. 24002-24002.View/Download from: Publisher's site
Intracellular membrane nanotube formation and its dynamics play important roles for cargo transportation and organelle biogenesis. Regarding the regulation mechanisms, while much attention has been paid on the lipid composition and its associated protein molecules, effects of the vesicle size has not been studied in the cell. Giant unilamellar vesicles (GUVs) are often used for in vitro membrane deformation studies, but they are much larger than most intracellular vesicles and the in vitro studies also lack physiological relevance. Here, we use lysosomes and autolysosomes, whose sizes range between 100 nm and 1 μm, as model systems to study the size effects on nanotube formation both in vivo and in vitro. Single molecule observations indicate that driven by kinesin motors, small vesicles (100-200 nm) are mainly transported along the tracks while a remarkable portion of large vesicles (500-1000 nm) form nanotubes. This size effect is further confirmed by in vitro reconstitution assays on liposomes and purified lysosomes and autolysosomes. We also apply Atomic Force Microscopy (AFM) to measure the initiation force for nanotube formation. These results suggest that the size-dependence may be one of the mechanisms for cells to regulate cellular processes involving membrane-deformation, such as the timing of tubulation-mediated vesicle recycling.
Li, R, Zhang, W, Su, QP, Xue, B & Sun, Y 2015, 'Structural and Functional Study of Midbody during Cytokinesis', BIOPHYSICAL JOURNAL, vol. 108, no. 2, pp. 631A-631A.View/Download from: Publisher's site
Li, Y, Liu, Z, Zhang, Y, Su, QP, Xue, B, Shao, S, Zhu, Y, Xu, X, Wei, S & Sun, Y 2015, 'Live-cell and super-resolution imaging reveal that the distribution of wall-associated protein A is correlated with the cell chain integrity of Streptococcus mutans.', Mol Oral Microbiol, vol. 30, no. 5, pp. 376-383.View/Download from: Publisher's site
Streptococcus mutans is a primary pathogen responsible for dental caries. It has an outstanding ability to form biofilm, which is vital for virulence. Previous studies have shown that knockout of Wall-associated protein A (WapA) affects cell chain and biofilm formation of S. mutans. As a surface protein, the distribution of WapA remains unknown, but it is important to understand the mechanism underlying the function of WapA. This study applied the fluorescence protein mCherry as a reporter gene to characterize the dynamic distribution of WapA in S. mutans via time-lapse and super-resolution fluorescence imaging. The results revealed interesting subcellular distribution patterns of WapA in single, dividing and long chains of S. mutans cells. It appears at the middle of the cell and moves to the poles as the cell grows and divides. In a cell chain, after each round of cell division, such dynamic relocation results in WapA distribution at the previous cell division sites, resulting in a pattern where WapA is located at the boundary of two adjacent cell pairs. This WapA distribution pattern corresponds to the breaking segmentation of wapA deletion cell chains. The dynamic relocation of WapA through the cell cycle increases our understanding of the mechanism of WapA in maintaining cell chain integrity and biofilm formation.
Mi, N, Chen, Y, Wang, S, Chen, M, Zhao, M, Yang, G, Ma, M, Su, Q, Luo, S, Shi, J, Xu, J, Guo, Q, Gao, N, Sun, Y, Chen, Z & Yu, L 2015, 'CapZ regulates autophagosomal membrane shaping by promoting actin assembly inside the isolation membrane.', Nat Cell Biol, vol. 17, no. 9, pp. 1112-1123.View/Download from: Publisher's site
A fundamental question regarding autophagosome formation is how the shape of the double-membrane autophagosomal vesicle is generated. Here we show that in mammalian cells assembly of an actin scaffold inside the isolation membrane (the autophagosomal precursor) is essential for autophagosomal membrane shaping. Actin filaments are depolymerized shortly after starvation and actin is assembled into a network within the isolation membrane. When formation of actin puncta is disrupted by an actin polymerization inhibitor or by knocking down the actin-capping protein CapZβ, isolation membranes and omegasomes collapse into mixed-membrane bundles. Formation of actin puncta is PtdIns(3)P dependent, and inhibition of PtdIns(3)P formation by treating cells with the PI(3)K inhibitor 3-MA, or by knocking down Beclin-1, abolishes the formation of actin puncta. Binding of CapZ to PtdIns(3)P, which is enriched in omegasomes, stimulates actin polymerization. Our findings illuminate the mechanism underlying autophagosomal membrane shaping and provide key insights into how autophagosomes are formed.
Wang, C, Du, W, Su, QP, Zhu, M, Feng, P, Li, Y, Zhou, Y, Mi, N, Zhu, Y, Jiang, D, Zhang, S, Zhang, Z, Sun, Y & Yu, L 2015, 'Dynamic tubulation of mitochondria drives mitochondrial network formation.', Cell Res, vol. 25, no. 10, pp. 1108-1120.View/Download from: Publisher's site
Mitochondria form networks. Formation of mitochondrial networks is important for maintaining mitochondrial DNA integrity and interchanging mitochondrial material, whereas disruption of the mitochondrial network affects mitochondrial functions. According to the current view, mitochondrial networks are formed by fusion of individual mitochondria. Here, we report a new mechanism for formation of mitochondrial networks through KIF5B-mediated dynamic tubulation of mitochondria. We found that KIF5B pulls thin, highly dynamic tubules out of mitochondria. Fusion of these dynamic tubules, which is mediated by mitofusins, gives rise to the mitochondrial network. We further demonstrated that dynamic tubulation and fusion is sufficient for mitochondrial network formation, by reconstituting mitochondrial networks in vitro using purified fusion-competent mitochondria, recombinant KIF5B, and polymerized microtubules. Interestingly, KIF5B only controls network formation in the peripheral zone of the cell, indicating that the mitochondrial network is divided into subzones, which may be constructed by different mechanisms. Our data not only uncover an essential mechanism for mitochondrial network formation, but also reveal that different parts of the mitochondrial network are formed by different mechanisms.
Wang, G, Li, Y, Wang, P, Liang, H, Cui, M, Zhu, M, Guo, L, Su, Q, Sun, Y, McNutt, MA & Yin, Y 2015, 'PTEN regulates RPA1 and protects DNA replication forks', CELL RESEARCH, vol. 25, no. 11, pp. 1189-1204.View/Download from: Publisher's site
Liu, Z, Xing, D, Su, QP, Zhu, Y, Zhang, J, Kong, X, Xue, B, Wang, S, Sun, H, Tao, Y & Sun, Y 2014, 'Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space', Nature Communications, vol. 5, pp. 1-8.View/Download from: Publisher's site
Imaging the location and dynamics of individual interacting protein pairs is essential but often difficult because of the fluorescent background from other paired and non-paired molecules, particularly in the sub-diffraction cellular space. Here we develop a new method combining bimolecular fluorescence complementation and photoactivated localization microscopy for super-resolution imaging and single-molecule tracking of specific protein–protein interactions. The method is used to study the interaction of two abundant proteins, MreB and EF-Tu, in Escherichia coli cells. The super-resolution imaging shows interesting distribution and domain sizes of interacting MreB–EF-Tu pairs as a subpopulation of total EF-Tu. The single-molecule tracking of MreB, EF-Tu and MreB–EF-Tu pairs reveals intriguing localization-dependent heterogonous dynamics and provides valuable insights to understanding the roles of MreB–EF-Tu interactions.