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Imaging signaling protein complexes in live immune cells at the single molecule level using total internal reflection fluorescence microscopy

Thursday, October 27, 2011 — Core Poster Session

10:00 a.m. – Noon

South Lobby of Building 10




  • JA Brzostowski
  • X Xu
  • T Meckel
  • P Tolar
  • HW Sohn
  • W Liu
  • D Liu
  • CC Gross
  • E Martinez
  • EO Long
  • T Jin
  • SK Pierce


Total internal reflection fluorescence microscopy (TIRFM) is a spatially limited, high contrast imaging technique that eliminates the bulk cytosolic fluorescent signal from the imaging plane. The ~100 nm penetration depth of the excitation beam allows for visualization of fluorophores down to the single molecule level at or near the plasma membrane. Combined with particle tracking algorithms, TIRFM is an exceptional technique to explore the fundamental mechanisms of signaling biology in live cells. Presented are recent examples from our laboratory using TIRFM to study the signaling mechanisms of the B cell receptor, a G protein coupled receptor that mediates chemotaxis, and cell surface proteins that regulate natural killer cell targeting.

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