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The Golgi apparatus (/ ˈ ɡ ɒ l dʒ i /), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. [1] Part of the endomembrane system in the cytoplasm , it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination.
The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis. [ 6 ]
The Coat Protein Complex II, or COPII, is a group of proteins that facilitate the formation of vesicles to transport proteins from the endoplasmic reticulum to the Golgi apparatus or endoplasmic-reticulum–Golgi intermediate compartment.
Electron micrograph of in vitro–formed COPI-coated vesicles. Average vesicle diameter at the membrane level is 60 nm. COPI is a coatomer, a protein complex [1] that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments.
It is located on the trans face of the Golgi apparatus and is made up of cisternae. The cisternae play a crucial role in the packaging, modification, and transport functions for the cell overall. The proteins and polysaccharides that get processed here within the cisterna will then be sent to their specified locations. [3]
The transitional ER gets its name because it contains ER exit sites. These are areas where the transport vesicles which contain lipids and proteins made in the ER, detach from the ER and start moving to the Golgi apparatus. Specialized cells can have a lot of smooth endoplasmic reticulum and in these cells the smooth ER has many functions. [6]
The endoplasmic-reticulum–Golgi intermediate compartment (ERGIC) is an organelle in eukaryotic cells. This compartment mediates transport between the endoplasmic reticulum (ER) and Golgi complex, facilitating the sorting of cargo. [1] The cluster was first identified in 1988 using an antibody to the protein that has since been named ERGIC-53. [2]
The protein normally resides in a cell structure called the Golgi apparatus, which modifies and transports newly produced enzymes and other proteins. Here, ATP7A supplies Cu(I) to certain enzymes (e.g. peptidyl-α-monooxygenase , tyrosinase , and lysyl oxidase [ 9 ] ) that are critical for the structures and functions of brain, bone, skin, hair ...