Golgi apparatus (redirected from Golgicomplex)

Golgi apparatus [′gȯl‚jē ‚ap·ə‚rad·əs]

(cell nad molecular biology)

A cellular organelle that is part of the cytoplasmic membrane system; it is composed of regions of stacked cisternae and it functions in secretory processes.

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Golgi apparatus

An organelle, named after the Italian histologist Camillo Golgi, found in all eukaryotic cells but absent from prokaryotes such as bacteria. It consists of flattened membrane-bounded compartments known as cisternae. In most cells, the Golgi cisternae are organized into stacks. Different cell types contain from one to several thousand Golgi stacks. The Golgi apparatus sorts newly synthesized proteins for delivery to various destinations, and modifies the oligosaccharide chains found on glycoproteins and glycolipids. See Cell organization

The Golgi apparatus acts at an intermediate stage in the secretory pathway. A subset of the proteins synthesized by the cell are inserted into the endoplasmic reticulum. Most such proteins are then delivered to the Golgi apparatus by means of coat protein II (COPII) transport vesicles, which form at endoplasmic reticulum exit sites. Newly synthesized proteins traverse the Golgi stack until they reach the trans-most Golgi compartment, which is termed the trans-Golgi network to connote its extensive tubulation. The trans-Golgi network sorts the proteins into several types of vesicles. Clathrin-coated vesicles carry certain proteins to lysosomes. Other proteins are packaged into secretory vesicles for immediate delivery to the cell surface. Still other proteins are packaged into secretory granules, which undergo regulated secretion in response to specific signals. This sorting function of the Golgi apparatus allows the various organelles to grow while maintaining their distinct identities. See Cell membranes, Endoplasmic reticulum, Lysosome

The best understood of the processing reactions carried out by the Golgi apparatus is the remodeling of oligosaccharides (chains of six-carbon sugars) that are attached to glycoproteins. During insertion of a newly synthesized protein into the endoplasmic reticulum, one or more copies of a 14-sugar oligosaccharide may be attached to the amino acid asparagine at specific locations in the polypeptide chain. As the protein passes through the Golgi stack, the asparagine-linked oligosaccharides are modified to generate a diverse range of structures. Additional oligosaccharides may become linked to the amino acids serine and threonine. Although the particular oligosaccharide modifications are quite different in animal, plant, and fungal cells, the Golgi apparatus always functions as a “carbohydrate factory.” See Oligosaccharide

The Golgi apparatus also carries out other processing events, including the addition of sulfate groups to the amino acid tyrosine in some proteins, the cleavage of protein precursors to yield mature hormones and neurotransmitters, and the synthesis of certain membrane lipids such as sphingomyelin and glycosphingolipids. See Lipid, Protein