I'm hoping to express several proteins to form a complex and get exocytosed or put onto the outer plasma membrane.
Is there a signal peptide or some process I can exploit to get the whole complex sent to the outside AFTER assembly? As I understand it, TM domains would send an individually tagged component to the membrane, not the entire complex.
I realize this is a long-shot and the answer will probably be "depends" but I wanted to not miss an obvious answer.
You may use signal peptides in single proteins but not for "exocytosis" of protein complexes.
Single proteins carrying a signal peptide are directly translated into the lumen of the endoplasmic reticulum (rough ER) and may be directed via the golgi to the outer cell membrane or other cell compartments such as lysosomes dependent on their structural properties (for example attached and modified carbohydrate components). If a protein complex should be exported to the outher membrane it has to be formed at least in the golgi apparatus. This means that all components have to be present there. I recommend to study the biosynthesis of collagen as triple helix (biochemistry textbooks). I hope you can get an idea of the mechanisms and perhaps a solution to your question.
Best wishes, Peter
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