Regulation of protein transport and neuroendocrine secretion by the ARF1-PKD complex at the Trans-Golgi network

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The serine/threonine protein kinase D (PKD) family regulates various cellular functions including the fission of transport carriers at the Trans Golgi network (TGN). Thus, PKDs control a central mecha-nism that is crucial for both constitutive and regulated secretion. This mechanism can even constitute a therapeutic target, e.g. in hypersecretory states, such as the Carcinoid syndrome as we have shown previously. However, the precise mechanisms by which PKDs regulate the fission of transport carriers at the TGN are still incompletely understood. Previously we have shown that PKDs interact with ARF GTPases and that this interaction is required for their function at the TGN. In this proposal we will de-termine the precise role of the interaction between ARF1 and PKDs at the TGN and identify further interacting proteins and potential effectors leading to vesicle shedding at the TGN using state of the art techniques including peptide mass fingerprint analysis.