Honors College Thesis

 

Characterization of Fer1L6 lipid binding properties and its expression in cell cycle Public Deposited

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https://ir.library.oregonstate.edu/concern/honors_college_theses/z603r354h

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  • Ferlins are a family of calcium-sensitive proteins involved in fusion and fission membrane trafficking events. There are six ferlin members: dysferlin, otoferlin, myoferlin, Fer1L4, Fer1L5, and Fer1L6. Previous research shows the first three ferlins play a pathophysiological role in humans, while the other three remain uncharacterized. Fer1L6 is one of the three uncharacterized proteins, but studies in our lab suggest that it may play a role in muscle development in zebrafish. Fer1L6 contains five C2 domains that bind calcium ions and target the protein to membranes. However, to understand how Fer1L6 deficiency disrupts normal muscle development, we must understand how the protein interacts with lipids. To gain insight into how Fer1L6 functions, laurdan fluorescence assays, co-sedimentation assay, and cell culture studies were performed. Our assays show that the C2 domains of Fer1L6 exhibit electrostatic and hydrophobic interactions similar to those seen in the other ferlins. In addition, the domains of Fer1L6 prefer to bind to negatively charged phospholipids, implying that Fer1L6 may localize to plasma membrane or Golgi apparatus. Our study also indicates Fer1L6 is highly expressed in the G2 stage of the cell cycle. Understanding each domain’s lipid-binding affinity, our next step is to construct truncated and full-length Fer1L6 and investigate their effects on lipid binding.
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  • OSU Summer Undergraduate Research Experience Fellowship
  • OSU Undergraduate Research, Innovation, Scholarship & Creativity
  • OSU Cripps Undergraduate Research Experience (CURE) Summer Fellowship
  • OSU Undergraduate Research, Scholarship, and the Arts-ENGAGE (URSA-ENGAGE)
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  • Ongoing Research
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  • 2018-05-14 to 2019-06-15

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