Belmont University Research Symposium (BURS)

Publication Date

2024

College

Sciences and Mathematics, College of

Department

Chemistry and Physics, Department of

BURS Faculty Advisor

Rebecca Adams

Presentation Type

Oral Presentation

Abstract

The mechanisms of how mechanical stress is translated into cellular action and structural reorganization within the nuclear envelope are largely unexplored. The Linker of Nucleoskeleton and Cytoskeleton (LINC) complex is a transmembrane protein complex that connects the actin cytoskeleton to the lamin nucleoskeleton, enabling mechanical forces to be translated between the cytoplasm and the nucleus. A better understanding of the translation of physical forces into cell responses can be gained through confirming the existence of interactions between LINC complex proteins and nuclear pore complexes (NPCs), which control the exchange of biochemical signals and macromolecules in and out of the nucleus through mRNA export. An interaction between NPC protein Ndj1 and LINC complex protein Mps3, was determined by transforming sequences for Venus split-green fluorescent protein (GFP) into the genomes of S. cerevisiae models so as to tag the NPC and LINC proteins. Fluorescent microscopy of Venus-tagged cells that were not subjected to any sort of mechanical stress did not fluoresce. Results for Venus-tagged yeast that were centrifuged at 13,000 rpm for one minute, however, showed fluorescence that indicated localizations around the nucleus, confirming the interaction between Ndj1 and Mps3 on the inner nuclear envelope.

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