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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 (also known as the Golgi body and the Golgi complex) is composed of separate sacs called cisternae. Its shape is similar to a stack of pancakes. The number of these stacks varies with the specific function of the cell. The Golgi apparatus is used by the cell for further protein modification.
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.
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 ]
Prokaryotes have fewer organelles than eukaryotes. Both have plasma membranes and ribosomes (structures that synthesize proteins [clarification needed] and float free in cytoplasm). Two unique characteristics of prokaryotes are fimbriae (finger-like projections on the surface of a cell) and flagella (threadlike structures that aid movement). [2]
The Golgi apparatus plays a pivotal role in N-linked glycosylation, a process that begins in the ER and is elaborated within the Golgi. Through the sequential trimming and addition of sugars like GlcNAc, mannose, galactose, and sialic acid, the Golgi ensures that proteins are properly modified for their final functional roles.
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 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]