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By coupling target recognition to receptor\u2010mediated uptake, LYTACs exploit endogenous trafficking pathways to access disease\u2010associated proteins beyond the reach of conventional intracellular degradation mechanisms. Related target\u2010intrinsic and cross\u2010linking\u2010driven strategies can likewise promote lysosomal target delivery without recruiting a separate clearance receptor. However, target internalization alone does not establish productive degradation. Following entry, target\u2010containing complexes encounter a competitive endosomal network in which they may recycle, undergo retrograde transport or transcytosis, remain in non\u2010degradative compartments, or proceed to lysosomes. Here, we present a routing\u2010centered framework for understanding and designing extracellular and membrane\u2010protein degradation. We discuss how target biology, receptor choice, tissue distribution, ligand competition, signaling liability, molecular architecture, and intracellular sorting shape degrader performance. We also outline evidence standards for distinguishing bona fide lysosome\u2010dependent target loss from surface depletion, redistribution, epitope masking, shedding, secretion blockade, transcriptional effects, and nonspecific toxicity. 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