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C-Myc, N-Myc and L-Myc were shown to have a partially redundant function in cells. Since their
identification, extensive efforts were made to characterize their respective function at homeostasis and
their role in various infamous diseases. Still, very little is known about those proteins at a biophysical level,
except for c-MYC. Interestingly, despite being critical for their function, the three proteins present
significant difference in their Leucine Zipper (bHLHLZ).
With this short study, we propose to leverage our experience in bHLHLZ purification and biophysics to study
and compare the bHLHLZ of MYC, MYCL and MYCN with a special focus on the characterization of their
oligomeric state and their capacity to bind DNA and Max, MYC obligate partner. Through biochemical and
biophysical techniques, we aim to understand how the differences of charge and sequence can affect their
behavior and function.
During the first part of the project, the student will acquire competences in protein recombinant expression
and purification by IEC and / or affinity chromatography. He/she will then have the opportunity to develop
skills in biochemical and biophysical assays (ELISA, circular dichroism, Differential Scanning Fluorimetry,
Electro-Mobility Shift Assay, among others). Finally, the student will have the opportunity to test his/her
findings in biologically-relevant experimental models.
Pierre Lavigne
Universitat Autònoma de Barcelona
Life Sciences
Health and Related Sciences & Technology; Pharmaceuticals
Université de Sherbrooke
Globalink Research Award
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