Coatomer
The coatomer is a protein complex that coats membrane-bound transport vesicles. Two types of coatomers are known: *COPI (retrograde transport from trans-Golgi network to cis-Golgi network and endoplasmic reticulum) *COPII (anterograde transport from ER to the cis-Golgi) Coatomers are functionally analogous and evolutionarily homologous to clathrin adaptor proteins, also known as adaptins, which regulate endocytosis from the plasma membrane and transport from the trans-Golgi network to lysosomes. Structure The coatomer protein complex is made up of seven nonidentical protein subunits. These seven nonidentical protein subunits are part of two protein subcomplexes. The first subcomplex consists of Ret1(α-COP), Sec27(β’-COP), and Sec 28(ε-COP). The second subcomplex consists of Sec26 (β-COP), Sec21 (γ-COP), Ret2(δ-COP), and Ret3 (ζ-COP). COP I COPI is a coatomer that coats the vesicles transporting proteins from the Golgi complex to the ER. This pathway is referred t ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
COPI
COPI is a coatomer, a protein complex 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. 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, δ, ε and 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. COPI consists of seven subunits which compose the hetero ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid resid ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Alpha Helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues earlier along the protein sequence. The alpha helix is also called a classic Pauling–Corey–Branson α-helix. The name 3.613-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most extreme and the most predictable from sequence, as well as the most prevalent. Discovery In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching. The data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of ≈. Astbu ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
SEC31A
Protein transport protein Sec31A is a protein that in humans is encoded by the ''SEC31A'' gene. The protein encoded by this gene is similar to the SEC31 protein from yeast Yeasts are eukaryotic, single-celled microorganisms classified as members of the fungus kingdom. The first yeast originated hundreds of millions of years ago, and at least 1,500 species are currently recognized. They are estimated to consti .... The yeast SEC31 protein is known to be a component of the COPII protein complex, which is responsible for vesicle budding from endoplasmic reticulum (ER). This protein was found to colocalize with SEC13, one of the other components of COPII, in the subcellular structures corresponding to the vesicle transport function. An immunodepletion experiment confirmed that this protein is required for ER-Golgi transport. Alternative splicing results in multiple transcript variants encoding different isoforms. Halperin-Birk syndrome (HLBKS), a rare autosomal recessive ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
SEC24A
SEC24 family, member A (S. cerevisiae) is a protein that in humans is encoded by the ''SEC24A'' gene. The protein belongs to a protein family that are homologous to yeast Sec24. It is a component of coat protein II ( COPII)-coated vesicles that mediate protein transport from the endoplasmic reticulum. Model organisms Model organisms have been used in the study of SEC24A function. A conditional knockout mouse line, called ''Sec24atm1a(KOMP)Wtsi'' was generated as part of the International Knockout Mouse Consortium The International Knockout Mouse Consortium (IKMC) is a scientific endeavour to produce a collection of mouse embryonic stem cell lines that together lack every gene in the genome, and then to distribute the cells to scientific researchers to crea ... program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists. Male and female animals underwent a standardized phenotypic screen to determine the ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
SEC23A
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 are ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Protein Dimer
In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", ''di-'' + '' -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins. A protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein-coupled cannabinoid receptors have the ability to form both homo- and heterodimers with sev ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Amphiphile
An amphiphile (from the Greek αμφις amphis, both, and φιλíα philia, love, friendship), or amphipath, is a chemical compound possessing both hydrophilic (''water-loving'', polar) and lipophilic (''fat-loving'') properties. Such a compound is called amphiphilic or amphipathic. Common amphiphilic substances are soaps, detergents, and lipoproteins. The phospholipid amphiphiles are the major structural component of cell membranes. Amphiphiles are the basis for a number of areas of research in chemistry and biochemistry, notably that of lipid polymorphism. Organic compounds containing hydrophilic groups at both ends of the molecule are called bolaamphiphilic. The micelles they form in the aggregate are prolate. Structure The lipophilic group is typically a large hydrocarbon moiety, such as a long chain of the form CH3(CH2)n, with n > 4. The hydrophilic group falls into one of the following categories: # charged groups #* anionic. Examples, with the lipophilic part of ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
SAR1A
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 areas ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
P24 Protein Family
P24 protein family is a group of transmembrane proteins that are major components of COPI and COPII-coated vesicles. The family is also known as EMP24/GP25L/p24 family and TMP21-like proteins. The latter naming was after transmembrane emp24 domain-containing protein 10 that was found in the human brain. It was claimed to block the beta-amyloid peptide, which is implicated in the pathogenesis of Alzheimer's disease. Function p24 family proteins localize to the major organelles of the early secretory pathway: the endoplasmic reticulum and the Golgi apparatus, where they seem to be involved in trafficking between the two compartments. In yeast, all p24 family proteins can be removed, causing only a mild phenotype. However, in mammals at least some p24 proteins are essential for survival, e.g. removal of p24δ1 is lethal in mice. p24 family members have been implicated in the biogenesis of COPI and COPII-coated vesicles, transporting membrane-bound proteins through the secretory ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Lumen (anatomy)
In biology, a lumen (plural lumina) is the inside space of a tubular structure, such as an artery or intestine. It comes . It can refer to: *The interior of a vessel, such as the central space in an artery, vein or capillary through which blood flows. *The interior of the gastrointestinal tract *The pathways of the bronchi in the lungs *The interior of renal tubules and urinary collecting ducts *The pathways of the female genital tract, starting with a single pathway of the vagina, splitting up in two lumina in the uterus, both of which continue through the Fallopian tubes In cell biology, a lumen is a membrane-defined space that is found inside several organelles, cellular components, or structures: *thylakoid, endoplasmic reticulum, Golgi apparatus, lysosome, mitochondrion, or microtubule Transluminal procedures ''Transluminal procedures'' are procedures occurring through lumina, including: * Natural orifice transluminal endoscopic surgery in the lumina of, for example, ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |