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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 function and significance of vacuoles varies greatly according to the type of cell in which they are present, having much greater prominence in the cells of plants, fungi and certain protists than those of animals and bacteria. In general, the functions of the vacuole include: Isolating materials that might be harmful or a threat to the cell
Golgi apparatus: The primary function of the Golgi apparatus is to process and package the macromolecules such as proteins and lipids that are synthesized by the cell. Lysosomes and peroxisomes: Lysosomes contain digestive enzymes (acid hydrolases). They digest excess or worn-out organelles, food particles, and engulfed viruses or bacteria.
Golgi cell circuit functions also seem to be regulated by metabotropic glutamate receptors. Golgi cells possess mGluR2 receptors, [ 12 ] and when these receptors are activated, an inward rectifier K current is enhanced, aiding in the Golgi cell's silencing after a period of intensive granule cell-Golgi cell transmission. [ 13 ]
The proteins contain a signal sequence that allows the Golgi apparatus to recognize and direct it to the correct place. Golgi apparatus also produce glycoproteins and glycolipids. [21] Lysosome: The lysosome functions to degrade material brought in from the outside of the cell or old organelles. This contains many acid hydrolases, proteases ...
The number of cisterna in the Golgi stack is dependent on the organism and cell type. [3] The structure, composition, and function of each of the cisternae may be different inside the Golgi stack. These different variations of Golgi cisternae are categorized into 3 groups; cis Golgi network, medial, and trans Golgi network. [2]
The Golgi matrix is a collection of proteins involved in the structure and function of the Golgi apparatus. [1] [2] [3] The matrix was first isolated in 1994 as an amorphous collection of 12 proteins that remained associated together in the presence of detergent (which removed Golgi membranes) and 150 m M NaCl (which removed weakly associated proteins). [4]
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 ]