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Investigation of the Propensity for Self-Association of the N-Terminal Domain of Annexin A2 in the Presence of Anionic Lipids

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Annexin A2 (ANXA2), a calcium-dependent membrane binding protein shown to promote membrane domain formation, is implicated in many cellular processes. In order to determine if ANXA2 promotes domain formation by self-associating with the N-terminal domain of adjacent ANXA2 proteins upon binding anionic phospholipids, Forster Resonance Energy Transfer (FRET) assays were performed using ANXA2 proteins fluorescently labeled at the singular, exposed N-terminal cysteine residue. No FRET transfer was observed, suggesting that under these experimental conditions the N-terminal domains do not interact.

  • This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.
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  • E-project-042417-210748
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  • 2017
Date created
  • 2017-04-24
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