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Cisternae
A cisterna (: cisternae) is a flattened membrane vesicle found in the endoplasmic reticulum and Golgi apparatus. Cisternae are an integral part of the packaging and modification processes of proteins occurring in the Golgi. Function Proteins begin on the cis side of the Golgi (the side facing the ER) and exit on the trans side (the side facing the plasma membrane). Throughout their journey in the cisternae, the proteins are packaged and are modified for transport throughout the cell. The number of cisternae in the Golgi stack is dependent on the organism and cell type. 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 three groups; cis Golgi network, medial, and trans Golgi network. The ''cis'' Golgi network is the first step in the cisternal structure of a protein being packaged, while the ''trans'' Golgi network is the last step in the cisternal structure w ...
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Golgi Apparatus
The Golgi apparatus (), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic Cell (biology), cells. Part of the endomembrane system in the cytoplasm, it protein targeting, packages proteins into membrane-bound Vesicle (biology and chemistry), vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and Endocytosis, endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus. The Golgi apparatus was identified in 1898 by the Italian biologist and pathologist Camillo Golgi. The organelle was later named after him in the 1910s. Discovery Because of its large size and distinctive structure, the Golgi apparatus was one of the first organelles to be discovered and observed in detail. It was d ...
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Golgi Apparatus (editors Version)
The Golgi apparatus (), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. 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. It resides at the intersection of the secretory, lysosomal, and endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus. The Golgi apparatus was identified in 1898 by the Italian biologist and pathologist Camillo Golgi. The organelle was later named after him in the 1910s. Discovery Because of its large size and distinctive structure, the Golgi apparatus was one of the first organelles to be discovered and observed in detail. It was discovered in 1898 by Italian physician Camillo Golgi during an investigation ...
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Glycosylation
Glycosylation is the reaction in which a carbohydrate (or ' glycan'), i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor) in order to form a glycoconjugate. In biology (but not always in chemistry), glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation (also 'non-enzymatic glycation' and 'non-enzymatic glycosylation') may refer to a non-enzymatic reaction. Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the ''O''-GlcNAc modification. Aglycosylation is a feature of engineered antibodies to bypass glycosylation. Five classes of glycans are produced: * ''N''-linked glycans attached to a nitrogen of asparagi ...
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Membrane
A membrane is a selective barrier; it allows some things to pass through but stops others. Such things may be molecules, ions, or other small particles. Membranes can be generally classified into synthetic membranes and biological membranes. Biological membranes include cell membranes (outer coverings of cells or organelles that allow passage of certain constituents); nuclear membranes, which cover a cell nucleus; and tissue membranes, such as mucous membrane, mucosae and serous membrane, serosae. Synthetic membranes are made by humans for use in laboratory, laboratories and industry (such as chemical plants). This concept of a membrane has been known since the eighteenth century but was used little outside of the laboratory until the end of World War II. Drinking water supplies in Europe had been compromised by The War and membrane filters were used to test for water safety. However, due to the lack of reliability, slow operation, reduced selectivity and elevated costs, membran ...
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Mannose-6-phosphate
Mannose-6-phosphate (M6P) is a molecule bound by lectin in the immune system. M6P is converted to fructose 6-phosphate by mannose phosphate isomerase. M6P is a key targeting signal for acid hydrolase precursor proteins that are destined for transport to lysosomes. The M6P tag is added to such proteins in the ''cis''-Golgi apparatus The Golgi apparatus (), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic Cell (biology), cells. Part of the endomembrane system in the cytoplasm, it protein targeting, packages proteins .... Specifically, in a reaction involving uridine diphosphate (UDP) and ''N''-acetylglucosamine, the enzyme N-acetylglucosamine-1-phosphate transferase catalyzes the ''N''-linked glycosylation of asparagine residues with M6P. Once appropriately marked with the M6P targeting signal, these proteins are moved to the ''trans''-Golgi network. There, the M6P moiety is recognized and bound by mannose 6-p ...
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COPI
COPI is a coatomer, a protein complex that coats vesicle (biology), vesicles transporting proteins from the ''cis'' end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally Translation (genetics), synthesized, and between Golgi compartments. This type of transport is ''retrograde transport'', in contrast to the ''anterograde transport'' associated with the COPII protein. The name "COPI" refers to the specific coat protein complex that initiates the budding process on the ''cis''-Golgi membrane. The coat consists of large protein subcomplexes that are made of seven different protein subunits, namely α, β, β', γ, Archain, δ, ε and COPZ1, ζ. Coat proteins Coat protein, or COPI, is an ADP ribosylation factor (ARF)-dependent protein involved in membrane traffic. COPI was first identified in retrograde traffic from the ''cis''-Golgi to the rough endoplasmic reticulum (ER) and is the most extensively studied of ARF-dependent adaptors. ...
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COPII
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. This process is termed anterograde transport, in contrast to the retrograde transport associated with the COPI complex. COPII is assembled in two parts: first an inner layer of Sar1, Sec23, and Sec24 forms; then the inner coat is surrounded by an outer lattice of Sec13 and Sec31. Function The COPII coat is responsible for the formation of vesicles from the endoplasmic reticulum (ER). These vesicles transport cargo proteins to the Golgi apparatus (in yeast) or the endoplasmic-reticulum-Golgi intermediate compartment (ERGIC, in mammals). Coat assembly is initiated when the cytosolic Ras GTPase Sar1 is activated by its guanine nucleotide exchange factor Sec12. Activated Sar1-GTP inserts itself into the ER membrane, binding preferentially to ...
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Protein Secretion
A secretory protein is any protein, whether it be endocrine or exocrine, which is secreted by a cell. Secretory proteins include many hormones, enzymes, toxins, and antimicrobial peptides. Secretory proteins are synthesized in the endoplasmic reticulum. Production The production of a secretory protein starts like any other protein. The mRNA is produced and transported to the cytosol where it interacts with a free cytosolic ribosome. The part that is produced first, the N-terminal, contains a signal sequence consisting of 6 to 12 amino acids with hydrophobic side chains. This sequence is recognised by a cytosolic protein, SRP (Signal Recognition Particle), which stops the translation and aids in the transport of the mRNA-ribosome complex to an SRP receptor found in the membrane of the endoplasmic reticulum. When it arrives at the ER, the signal sequence is transferred to the translocon, a protein-conducting channel in the membrane that allows the newly synthesized polypeptide to b ...
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Vesicle (biology And Chemistry)
In cell biology, a vesicle is a structure within or outside a cell, consisting of liquid or cytoplasm enclosed by a lipid bilayer. Vesicles form naturally during the processes of secretion ( exocytosis), uptake (endocytosis), and the transport of materials within the plasma membrane. Alternatively, they may be prepared artificially, in which case they are called liposomes (not to be confused with lysosomes). If there is only one phospholipid bilayer, the vesicles are called ''unilamellar liposomes''; otherwise they are called ''multilamellar liposomes''. The membrane enclosing the vesicle is also a lamellar phase, similar to that of the plasma membrane, and intracellular vesicles can fuse with the plasma membrane to release their contents outside the cell. Vesicles can also fuse with other organelles within the cell. A vesicle released from the cell is known as an extracellular vesicle. Vesicles perform a variety of functions. Because it is separated from the cytosol, the ...
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Mannosidase II
Mannosyl-oligosaccharide 1,3-1,6-α-mannosidase, also known as Golgi α-mannosidase II, is an enzyme with List of enzymes, systematic name ''(1→3)-(1→6)-mannosyl-oligosaccharide α-D-mannohydrolase''. It catalysis, catalyses the hydrolysis of the terminal (1→3)- and (1→6)-linked α-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3. This enzyme is involved in the synthesis of glycoproteins. It is a key enzyme of N-linked glycan, ''N''-linked glycan processing and is inhibited by small molecule swainsonine. References External links

* {{Portal bar, Biology, border=no EC 3.2.1 ...
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Mannosidase I
Mannosyl-oligosaccharide 1,2-α-mannosidase (, ''mannosidase 1A'', ''mannosidase 1B'', ''1,2-α-mannosidase'', ''exo-α-1,2-mannanase'', ''mannose-9 processing α-mannosidase'', ''glycoprotein processing mannosidase I'', ''mannosidase I'', ''Man9-mannosidase'', ''ManI'', ''1,2-α-mannosyl-oligosaccharide α-D-mannohydrolase'') is an enzyme with systematic name ''2-α-mannosyl-oligosaccharide α-D-mannohydrolase''. It catalyses the hydrolysis of the terminal (1→2)-linked α-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2. This enzyme is involved in the synthesis of glycoproteins Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known a .... Kifunensine is a potent inhibitor of mannosidase I. References External links * {{Portal bar, Biology, border=no EC ...
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