RESEARCH: MEMBRANE TRANSPORT
FOLDING PROJECT #17901 PROFILE

This project studies how adding phosphate groups to a sugar transporter's tail affects how it works and clumps together with other transporters. Understanding this helps us see how cells transport sugar differently when their metabolism changes.

Measuring the Effects of Post-translational Modification on Membrane Transporter Function and Oligomerization: Membrane transporters possess terminal tails which can variably regulate their substrate recognition, gating dynamics, and oligomerization (see https://royalsocietypublishing.org/doi/full/10.1098/rsob.190083 for a review).

To reflect physiological conditions and satisfy the instantaneous demands of cells, these termini are known to be post-translationally modified (PTM).

PTMs, like phosphorylation, have been shown to regulate transporter function through allostery or direct local interactions, thus blocking transmembrane substrate import and/or export. Simulations in this project will be focused on studying how C-terminal phosphorylation affects oligomerization dynamics of a sugar transporter.

While a basic protein folding problem, understanding how PTMs affect transporter oligomerization, and oligomer dynamics, is critical for understanding biological regulations for basal transport activity.

This study's ability to observe how terminal PTMs may influence sugar transport dynamics has implications for studying cells in altered metabolic states.

Post-translational Modification

Chemical changes to proteins after synthesis.

Post-translational modifications (PTMs) are chemical alterations that occur to proteins after they have been synthesized. These modifications can include phosphorylation, glycosylation, and ubiquitination, and they play a crucial role in regulating protein function, localization, and interactions.

Membrane Transporter

Proteins embedded in cell membranes that facilitate the movement of molecules across.

Membrane transporters are specialized proteins found within cell membranes. They act as gatekeepers, selectively allowing specific molecules to pass through the membrane and into or out of the cell. This process is essential for maintaining cellular homeostasis and enabling various biological functions.

Oligomerization

The process of multiple protein molecules joining together.

Oligomerization is the process by which individual protein molecules assemble into larger complexes called oligomers. This interaction can significantly influence protein function, stability, and localization within the cell.

Phosphorylation

Adding a phosphate group to a molecule.

Phosphorylation is a crucial post-translational modification that involves the addition of a phosphate group to a molecule, typically a protein. This process often acts as a switch, regulating protein activity, interactions, and localization.

Allostery

Change in protein shape/function due to binding at a site other than the active site.

Allostery describes a phenomenon where binding of a molecule to one site on a protein influences its activity at a different, often distant, site. This regulation mechanism plays a vital role in controlling protein function and cellular processes.

Substrate

Molecule acted upon by an enzyme.

A substrate is the molecule that an enzyme acts upon to catalyze a specific chemical reaction. The enzyme binds to the substrate at its active site, facilitating the transformation of the substrate into products.