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Mark J. Uline, PhD, University of South Carolina

PROJECT TITLE: Membrane Curvature and Lipid Composition Synergize to Regulate N-RAS Anchor Recruitment

Proteins anchored to membranes through covalently linked fatty acids and/or isoprenoid groups play crucial roles in all forms of life. We recently showed that membrane shape/curvature can in itself mediate the recruitment of lipidated proteins. However, exactly how membrane curvature and composition synergize still remains largely unexplored.

This is a fundamental biophysics study that combines frontier experimental techniques with cutting-edge theoretical advances to elucidate the molecular mechanisms related to the sorting and trafficking of lipidated proteins. We focused this study on how lipid acyl chain saturation, lipid headgroup size, and acyl chain length modulate the capacity of membrane curvature to recruit lapidated proteins. Our findings suggest that the different compositions of cellular compartments could modulate the potency of membrane curvature to recruit lipidated proteins and thereby synergistically regulate the trafficking and sorting of lipidated proteins.

Funding for the theoretical component of the work was through the SC INBRE Developmental Research Project program. I am a target faculty. Funding for the project provided financial support for Celeste Kennard, my PhD student.


Publications as a result of the project:

  • Jannik B. Larsen, Celeste Kennard, Søren L. Pedersen, Knud J. Jensen, Mark J. Uline, Nikos S. Hatzakis, Dimitrios Stamou. Membrane Curvature and Lipid Composition Synergize To Regulate N-Ras Anchor Recruitment. Biophysical Journal, Volume 113, Issue 6, 19 September 2017, Pages 1269-1279 https://doi.org/10.1016/j.bpj.2017.06.051

May 26, 2018