Efforts towards characterizing the cellular surface proteome and secretome with the help of LC-MS approaches has proven to yield valuable resources for the identification of biomarkers as well as uncovering compositional changes upon perturbation and alteration of cellular homeostasis. Although comparative analyses are highly effective in revealing differences in protein abundances between separate conditions, they do not fully encompass potential effects that could manifest within the translation as well as shuttling of constituents that make up the plasma membrane proteome as well as the extracellular secretome. In order to investigate this additional aspect of proteostasis, this project established a time-resolved assay to measure the accumulation rates of newly synthesized proteins at and outside the cell surface over time. To this end, a cell surface capture approach (CSC) is combined with TMT-SILAC multiplexing to allow mass spectrometry-based time-resolved quantitation of newly-synthesized plasma membrane protein populations. Secretome samples harvested from cell culture supernatant are processed in a similar manner. We build upon a method previously established within our group called mePROD which enables quantification of proteins with a low heavy-to light ratios. With this approach, we hope to accurately delineate and characterize dynamic changes in cell surface proteome and secretome subpopulations upon general or specific cellular disturbance. Through establishing a bioinformatics analysis pipeline, we furthermore strive towards translating initial findings towards certain disease models in the future.