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The molecular post office inside the cell

e sequence as soon as the newly built protein chain leaves the ribosome. The SRP binds to the ribosome and directs it, together with the SRP receptor, to what is called the "translocon complex" in the membrane of the endoplasmic reticulum. The translocon complex is made of a "protein conducting channel" and other membrane proteins. The ribosome is anchored at the translocon and continues with protein biosynthesis.

Notable is that the ribosome can no longer bind to the translocon as soon as the SRP has bound to the ribosome. The ribosome needs additional support from the SRP receptor, which it transfers from the SRP to the translocon. Now that scientists understand the structure of the complex, they can see how the receptor interacts with ribosome and SRP and replaces parts of the SRP molecule. In this way, specific sites are made available for the translocon, which allows it to bind to the ribosome. Understanding this key event during protein sorting is essential to understanding how secretory and membrane proteins are expressed in a cell.


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Source:Max-Planck-Gesellschaft


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