Original title: Kinetic asymmetry drives directionality in an ATP-binding cassette transporter
Michael Rudolph, Hossein Batebi, Malavika Pramod, Katja Barth +4 · September 2026
Cells use tiny protein pumps called ABC transporters to move molecules across their membranes. Scientists did not know how fuel called ATP pushes these pumps to move in only one direction. Researchers studied this process and found two chemical bridges, called ionic locks, inside the protein. Here is how it works. A fuel unit called Mg 2+ -ATP acts like a key that breaks the inward-facing lock. This break powers the pump forward. After the fuel is used, the pump drops a piece called gamma-phosphate. This loss breaks the outward-facing lock, triggering the backward step. Because different parts of the pump become slow bottlenecks during the forward and backward steps, the pump moves in a set direction across this family of proteins.
Imagine a door with two latches, one on each side. To push it open you release the near latch, but the far latch still holds, so the door cannot swing back; releasing both at once just makes it sway. The trick is to release the near latch, push, and only then release the far latch. In this paper, the two latches are molecular locks inside a cellular pump: an energy molecule opens the first lock to start the forward motion, and after the energy is spent, losing a small chemical group opens the second lock, so the pump moves one way only.
ABC transporters are a large family of proteins that move molecules across cell membranes. This work explains how their one-way motion comes from two molecular locks that open in sequence. Because the same locks appear across the whole superfamily, the finding points to a shared design principle that could guide efforts to control these pumps.
The abstract doesn't say. It identifies the locks and proposes a mechanism, but it does not include experimental validation, direct structural evidence, or the identity of the specific transporter studied.
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Kinetic asymmetry drives directionality in an ATP-binding cassette transporter — Michael Rudolph, Hossein Batebi, Malavika Pramod et al. — bioRxiv — doi:10.64898/2026.09.11.751009
Abstract licence: CC BY
Explanation generated by Synthesis from the abstract — it is not the original paper. This is a preprint, so it hasn't necessarily been peer reviewed.