Research Partners
FBNP Imaging Partner
- Center for Biologic Imaging, University of Pittsburgh
- The University of Pittsburgh's Center for Biologic Imaging (CBI) provides centralized imaging services including light fluorescence microscopy, confocal laser scanning microscopy, electron microscopy, advanced computer-aided morphometry, and image analysis. The CBI's expertise in light and electron microscopy provides a glimpse into the tiniest of worlds, yielding big benefits for researchers. CBI prides itself on being a leading center in the application of cellular imaging from the single molecule to the whole animal.
FBNP Driving Biology Projects
- Quantifying the Translation of Single mRNAs in Living Cells.
Robert Singer, Albert Einstein College
- Our research is focused on understanding the expression and movement of RNA from transcription through nuclear export to localization in the cytoplasmic compartments such as the leading edge of a fibroblast, the bud tip of yeast or the axonal process of neurons.
- Small Molecule Discovery with HTS Multiplex Flow Cytometry and FAP Technology. Larry Sklar, University of New Mexico Center for Molecular Discovery (UNM-CMD)
- Unique screening platforms combining high-throughput flow cytometry and FAP technology have been successfully developed and validated for identifying small molecule regulators of protein‐protein interactions and receptor transport processes.
- Monitoring synaptic plasticity with cell surface selective biosensors that measure
the density of AMPA Receptor in cultured neurons and living animals. Pavel Osten, Cold Springs Harbor Laboratory
- Excitatory (glutamatergic) synaptic plasticity plays critical roles in many brain functions, including neurodevelopment, learning and memory, as well as in devastating diseases, such as autism spectrum disorders (ASD) and schizophrenia. Our goal is to develop a versatile, high‐throughput optical method to monitor AMPA receptor‐mediated excitatory synaptic plasticity.
- Functional Imaging of Microenvironment-induced Exocytosis of Cysteine Cathepsins from Invasive Cells.
Bonnie Sloane, Wayne State University
- Metabolic‐associated changes in the microenvironment such as hypoxia and the associated acidic pH alter trafficking and secretion of cysteine cathepsins, thereby augmenting cell invasion through increased pericellular proteolysis. To elucidate these processes we are developing new protease‐activated exocytosis biosensors and new protease biosensors.
- The Influence of Subunit Integrity on IgE Receptor Signaling.
Keith Lidke, University of New Mexico
- Our aim is to use FAP technology to quantify single molecule techniques for Single Particle Tracking (SPT) and Single Molecule Super-resolution. These methods will be used to determine how IgE binding stabilizes the multi-chain (αβγ2) FcεRI against disassembly.
- Intracellular FAP-based Biosensor Development.
Peter Berget, University of the Sciences, Philadelphia
Other TCNP collaborations
- Networks, Pathways and Dynamics of Lysine Modification
- The amino acid lysine is important in a wide range of biological processes, from control of gene expression to recycling of proteins. Lysine is unique among the amino acids because it can be modified in many ways, ranging from the addition of small functional groups to entire proteins, and these modifications have profound biological effects. For example, protein modification of lysines found on DNA-coiling histones is critical for epigenetic control of gene expression, which itself dictates the expression of the proteome in all cells. Other lysine modifications include acetylation, methylation, ubiquitylation and sumoylation. Among these, ubiquitylation is most well-understood; it controls proteins' life, death and trafficking, among other roles.
- New Tools for Exploring the Dynamic Interactome
- The National Center for Dynamic Interactome Research couples an established mass spectrometry resource, a cell biology / protein chemistry laboratory, a high-throughput systems biology resource, and a computational biology center. The Cell Biology and Biochemistry Core is supervised by Michael Rout, who is a pioneer in subcellular fractionation and the elucidation of macromolecular structures through the affinity purification of proteins. In particular, he is most noted for his studies on the nuclear pore complex and yeast spindle organizer.
NIH TCNP link
