The unhindered lateral mobility of a rhomboid intramembrane protease enables synapse remodelling
Synapses must maintain their stable molecular organisation while retaining the capacity to remodel in response to changing demands. In order to flexibly change synaptic strength, the abundance of trans-synaptic adhesion complexes needs to be modulated, yet how this is achieved is poorly understood. Here, we identify the rhomboid protease RHBDL2 as a membrane-immersed regulator of adhesion…
Synapses need to keep their stable molecular structure while still being able to change in response to new requirements. To achieve this flexibility in altering synaptic strength, the amount of trans-synaptic adhesion complexes has to be adjusted. However, the way this is accomplished remains unclear. Researchers have now discovered that a membrane-embedded enzyme called rhomboid protease, specifically RHBDL2, plays a key role as a regulator of these adhesion complexes.
What sets RHBDL2 apart is its ability to move freely across the neuronal surface without any restrictions. This unrestricted diffusion allows the enzyme to continuously scan the surface and eliminate unnecessary adhesion molecules through the permanent cleavage of their transmembrane domains. This process is essential for synapses to adapt their composition, both at rest and during active remodeling.
The importance of this function is highlighted by the fact that it is necessary for synapses to undergo changes during long term depression.
The study reveals an important mechanism that cells use to maintain functional signaling complexes in the membrane while selectively removing those proteins that are not essential.
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