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The Golgi apparatus modifies and sorts cargo arriving from the endoplasmic reticulum for delivery to other cellular destinations. The eponym refers to Camillo Golgi.

Its usual stacked organization is polarized: cargo enters on the cis side, encounters medial processing regions, and leaves through the trans side and trans-Golgi network. Golgi cisternae enclose a Golgi lumen separated from the surrounding cytosol. Processing changes cargo; sorting selects its destination.^[ref]

This division of labor explains why reaching the Golgi apparatus does not imply being secreted: cargo can take different onward routes, while resident enzymes continue working there. The conventional route discussed here is part of secretory protein routing; many cytosol proteins never enter it.

The Golgi lumen is the enclosed interior of a Golgi cisterna, distinct from the surrounding cytosol.

The membrane-sidedness rule in secretory protein routing still applies within the Golgi apparatus. For a local worked example, stipulate a membrane protein with a carbohydrate chain exposed to Golgi lumen and a tail exposed to cytosol. An enzyme confined to Golgi lumen can contact that chain, but cannot directly contact the cytosolic tail without a boundary-crossing step. A change in which Golgi cisterna contains the protein need not turn the protein over. Thus chemical accessibility and cargo location are different questions: moving cargo onward preserves its membrane sides under the budding and fusion operations described in secretory protein routing.

A lysosome is an acidic digestive and recycling organelle: one surrounding lipid bilayer encloses a lysosomal lumen containing acid hydrolases. These enzymes break down proteins, nucleic acids, carbohydrates and lipids by hydrolysis. Cargo can originate outside the biological cell, entering through endocytosis, or within its own cytoplasm, delivered through autophagy. Digestion therefore serves both disposal and reuse.^[ref]

An endosome sorts endocytosed cargo: some returns to the cell membrane, while some proceeds toward lysosomes. An autophagosome instead encloses material already in the cytoplasm. Both routes bring cargo into contact with digestive enzymes; neither implies that every internalized molecule is destroyed.^[ref]

Enzyme supply is a different itinerary from cargo disposal. Secretory protein routing and protein targeting deliver newly made digestive enzymes through the endoplasmic reticulum, Golgi apparatus and trans-Golgi network toward lysosomes.^[ref] The existing membrane transport and differential centrifugation articles explain the boundary-crossing and separation principles used below.

A proteasome is a different digestive machine: a protein complex without a surrounding lipid bilayer, acting on individual proteins in the cytosol and cell nucleus. Many targets carry ubiquitin chains. A lysosome accepts a much broader range of cargo, including material delivered inside an autophagosome. Thus an unwanted soluble protein and an unwanted mitochondrion pose different disposal problems; a proteasome does not swallow an intact mitochondrion.^[ref]

Secretory protein routing connects entry into the endoplasmic reticulum, protein folding and sorting, transfer to the Golgi apparatus, and delivery onward. In the conventional soluble-cargo route, transport vesicles carry lumenal contents between compartments; exocytosis releases cargo outside the cell membrane. Resident endoplasmic reticulum proteins can be retained or retrieved, and defective cargo can be held back. Many cytosol proteins never enter this route.^[ref]

The useful geometric rule is preservation of membrane sides: during budding and fusion, a lumen-facing region of a membrane protein stays lumen-facing, then faces the exterior after exocytosis; its cytosol-facing region stays cytosolic.^[ref]

Work through the schematic using two distinguishable labels A and B on a stipulated membrane protein. Start with A facing the ER lumen and B facing the cytosol. At each budding or fusion step, carry the surrounding membrane together with the labels; do not turn the protein over. The resulting pair is A facing the Golgi apparatus interior and B facing the cytosol, then A facing a transport vesicle interior and B facing the cytosol, and finally A facing the exterior and B facing the cytosol. This is a stepwise argument about the depicted operations, not a claim that the compartments have identical chemical contents. Likewise, once soluble cargo is inside the ER lumen, this schematic reaches the exterior with zero further crossings through a lipid bilayer: enclosed spaces join when membranes fuse. Delivery therefore need not mean repeatedly pushing a folded protein through a membrane.