Nicholas Toselli

Mentor: Dr. Michael Bubb
College of Medicine
 
"I got involved with research in the beginning of my sophomore year to strengthen my knowledge of molecular biology and biochemistry and help elucidate topics I was learning in the classroom. Working in the laboratory satisfies my scientific curiosity. I am able to use critical thinking skills and creativity to solve problems and progress through setbacks."

Major

Interdisciplinary Studies Biochemistry and Molecular Biology

Minor

N/A

Research Interests

  • Cytoskeleton Dynamincs
  • Apoptosis
  • Cancer Biology

Academic Awards

  • President's Honor Roll 2012-2015
  • Anderson Scholar 2014-2015
  • CLAS Dean's Office Scholarship 2015
  • University Scholars Program 2015-2016

Organizations

  • Health Outreach Quality Improvement Program
  • Pre-Health Diplomats
  • N/A

Volunteer

  • Mobile Outreach Clinic
  • St. Francis House
  • UF Health Shands

Hobbies and Interests

  • Soccer
  • Beach Volleyball
  • N/A
  • N/A

Research Description

The Effects on Alpha Adducin Function by a Proposed Auto-inhibitor
Adducin is a heterodimeric membrane-skeletal protein located at spectrin-actin junctions that connects the cytoskeleton and cell membrane of eukaryotic cells. Adducin plays a crucial role in assembly and regulation of actin filaments and of the spectrin-actin network. This research focuses on a proposed auto-inhibitor of alpha adducin, residues 586-701. Natively, the autoinhibitory domain of adducin is postulated to bind to the phosphorylation side domain (PSD) of adducin. It is hypothesized that spectrin binds to the autoinhibitory domain, thus releasing the phosphorylation site domain. As a result, actin is now able to bind to the phosphorylation site domain, activating adducin. A peptide that corresponds to alpha adducin from amino acid residue 586-701, will be cloned, expressed and purified. Assays of adducin function will be performed in vitro to check if the segment of alpha adducin inhibits adducin function. The functions of the PSD of adducin will be examined in the presence of spectrin-activated recombinant alpha adducin. Actin depolymerization rates capped by the adducin PSD will be compared in the presence and absence of the inhibitor. Adducin will be then be activated in living cells by expressing the auto-inhibitor peptide in a mammalian vector to determine the effect of inhibiting alpha adducin in vivo. The function being evaluated in these in vivo assays will be the regulation of Na+-K+-ATPase activity by adducin.