RESEARCH: MEMBRANE TRANSPORT
FOLDING PROJECT #17902 PROFILE

The project relates to studying how adding a phosphate group (phosphorylation) to the end of a sugar transporter protein affects how it works and clumps together with other proteins. This is important because these changes can control how much sugar enters and leaves cells, which is crucial for things like metabolism.

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

Alterations to a protein after its synthesis.

Post-translational modifications (PTMs) are chemical changes that happen to proteins *after* they've been made. These modifications can affect how proteins work, where they go in the cell, and how long they last. Examples include phosphorylation, glycosylation, and ubiquitination.

Membrane Transporter

A protein that moves molecules across cell membranes.

Membrane transporters are like tiny doors within cells that allow specific substances to enter or leave. These proteins play a crucial role in maintaining the balance of nutrients, ions, and waste products inside and outside the cell.

Oligomerization

The process of proteins coming together to form complexes.

Oligomerization is when multiple protein molecules join forces to create a larger, more complex structure. This can change how the proteins function and interact with other molecules.

Phosphorylation

The addition of a phosphate group to a molecule.

Phosphorylation is like attaching a tiny electrical switch to a protein. This can turn the protein 'on' or 'off', affecting its activity and interactions with other molecules.

Allostery

The regulation of a protein's activity by binding to a site other than the active site.

Allostery is like having a remote control for a protein. Binding to a specific site can change how the protein works, even if it's far from its main 'switch'.