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Adaptin
Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. The association between adaptins and clathrin are important for vesicular cargo selection and transporting. Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Therefore, adaptor proteins are responsible for the recruitment of cargo molecules into a growing clathrin-coated pits. The two major types of clathrin adaptor complexes are the heterotetrameric vesicular transport adaptor proteins (AP1-5), and the monomeric GGA (Golgi-localising, Gamma-adaptin ear homology, ARF-binding proteins) adaptors. Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between 16% and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
List Of Adaptins
Clathrin adaptor proteins, also known as adaptins, are proteins that mediate the formation of vesicles for intracellular trafficking and secretion. Adaptins are clustered subunits of adaptor protein (AP) complexes. There are several types of adaptin, each related to a different AP complex. Adaptins show sequence similarity to some COPI subunits, thus they are thought to have a common evolutionary origin. The adaptin is a heterotetramer consisting of two large adaptins (beta and one other depending on the complex), a medium adaptin (mu), and a small adaptin (sigma): * complex 1 ** AP1B1 ** AP1G1 AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the ''AP1G1'' gene. Function Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the tr ... ** AP1G2 ** AP1M1 ** AP1M2 ** AP1S1 ** AP1S2 *AP1S3* complex 2 ** AP2A1 ** AP2A2 ** AP2B1 ** AP2M1 ** AP2S1 * complex 3 ** AP3B ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AP2 Adaptor Complex
The AP2 adaptor complex is a multimeric protein that works on the cell membrane to internalize cargo in clathrin-mediated endocytosis. It is a stable complex of four adaptins which give rise to a structure that has a core domain and two appendage domains attached to the core domain by polypeptide linkers. These appendage domains are sometimes called 'ears'. The core domain binds to the membrane and to cargo destined for internalisation. The alpha and beta appendage domains bind to accessory proteins and to clathrin. Their interactions allow the temporal and spatial regulation of the assembly of clathrin-coated vesicles and their endocytosis. The AP-2 complex is a heterotetramer consisting of two large adaptins (α and β), a medium adaptin (μ), and a small adaptin (σ): * complex 2 ** AP2A1 (α unit 1) ** AP2A2 (α unit 2) ** AP2B1 (β unit) ** AP2M1 (μ unit) ** AP2S1 (σ unit) Structure The AP2 adaptor complex exists in two primary conformations: the open conformation (a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vesicular Transport Adaptor Protein
Vesicular transport adaptor proteins are proteins involved in forming complexes that function in the trafficking of molecules from one subcellular location to another. These complexes concentrate the correct cargo molecules in vesicles that bud or extrude off of one organelle and travel to another location, where the cargo is delivered. While some of the details of how these adaptor proteins achieve their trafficking specificity has been worked out, there is still much to be learned. There are several human disorders associated with defects in components of these complexes including Alzheimer's and Parkinson's diseases. The proteins Most of the adaptor proteins are heterotetramers. In the AP complexes, there are two large proteins ( ~100 k D) and two smaller proteins. One of the large proteins is termed β (beta), with β1 in the AP-1 complex, β2 in the AP-2 complex, and so on. The other large protein has different designations in the different complexes. In AP-1 i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Endocytosis
Endocytosis is a cellular process in which Chemical substance, substances are brought into the cell. The material to be internalized is surrounded by an area of cell membrane, which then buds off inside the cell to form a Vesicle (biology and chemistry), vesicle containing the ingested materials. Endocytosis includes pinocytosis (cell drinking) and phagocytosis (cell eating). It is a form of active transport. History The term was proposed by Christian de Duve, De Duve in 1963. Phagocytosis was discovered by Élie Metchnikoff in 1882. Pathways Endocytosis pathways can be subdivided into four categories: namely, receptor-mediated endocytosis (also known as clathrin-mediated endocytosis), caveolae, pinocytosis, and phagocytosis. * Clathrin-mediated endocytosis is mediated by the production of small (approx. 100 nm in diameter) vesicles that have a morphologically characteristic coat made up of the cytosolic protein clathrin. Clathrin-coated vesicles (CCVs) are found in vir ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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). COPI COPI is a coatomer that coats the vesicles transporting proteins from the Golgi complex to the ER. This pathway is ref ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lysosome
A lysosome () is a membrane-bound organelle that is found in all mammalian cells, with the exception of red blood cells (erythrocytes). There are normally hundreds of lysosomes in the cytosol, where they function as the cell’s degradation center. Their primary responsibility is catabolic degradation of proteins, polysaccharides and lipids into their respective building-block molecules: amino acids, monosaccharides, and free fatty acids. The breakdown is done by various enzymes, for example proteases, glycosidases and lipases. With an acidic lumen limited by a single-bilayer lipid membrane, the lysosome holds an environment isolated from the rest of the cell. The lower pH creates optimal conditions for the over 60 different Hydrolase, hydrolases inside. Lysosomes receive extracellular particles through endocytosis, and intracellular components through autophagy. They can also fuse with the plasma membrane and secrete their contents, a process called lysosomal exocytosis. After ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GABAA Receptor
The GABAA receptor (GABAAR) is an ionotropic receptor and ligand-gated ion channel. Its endogenous Ligand (biochemistry), ligand is γ-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the central nervous system. Accurate regulation of GABAergic transmission through appropriate developmental processes, specificity to neural cell types, and responsiveness to activity is crucial for the proper functioning of nearly all aspects of the central nervous system (CNS). Upon opening, the GABAA receptor on the Chemical synapse, postsynaptic cell is selectively permeable to Chloride, chloride ions () and, to a lesser extent, Bicarbonate, bicarbonate ions (). GABAAR are members of the ligand-gated ion channel receptor superfamily, which is a chloride channel family with a dozen or more heterotetrametric subtypes and 19 distinct subunits. These subtypes have distinct brain regional and subcellular localization, age-dependent expression, and the ability to undergo plastic alt ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Kinase
A protein kinase is a kinase which selectively modifies other proteins by covalently adding phosphates to them ( phosphorylation) as opposed to kinases which modify lipids, carbohydrates, or other molecules. Phosphorylation usually results in a functional change of the target protein ( substrate) by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. There are two main types of protein kinase. The great majority are serine/threonine kinases, which phosphorylate the hydroxyl groups of serines and threonines in their targets. Most of the others are tyrosine kinases, although additional types exist. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction. Chemical ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Organelle
In cell biology, an organelle is a specialized subunit, usually within a cell (biology), cell, that has a specific function. The name ''organelle'' comes from the idea that these structures are parts of cells, as Organ (anatomy), organs are to the Human body, body, hence ''organelle,'' the suffix ''-elle'' being a diminutive. Organelles are either separately enclosed within their own lipid bilayers (also called membrane-bounded organelles) or are spatially distinct functional units without a surrounding lipid bilayer (non-membrane bounded organelles). Although most organelles are functional units within cells, some functional units that extend outside of cells are often termed organelles, such as cilia, the flagellum and archaellum, and the trichocyst (these could be referred to as membrane bound in the sense that they are attached to (or bound to) the membrane). Organelles are identified by microscopy, and can also be purified by cell fractionation. There are many types of organe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Endosome
Endosomes are a collection of intracellular sorting organelles in eukaryotic cells. They are parts of the endocytic membrane transport pathway originating from the trans Golgi network. Molecules or ligands internalized from the plasma membrane can follow this pathway all the way to lysosomes for degradation or can be recycled back to the cell membrane in the endocytic cycle. Molecules are also transported to endosomes from the trans Golgi network and either continue to lysosomes or recycle back to the Golgi apparatus. Endosomes can be classified as early, sorting, or late depending on their stage post internalization. Endosomes represent a major sorting compartment of the endomembrane system in cells. Function Endosomes provide an environment for material to be sorted before it reaches the degradative lysosome. For example, low-density lipoprotein (LDL) is taken into the cell by binding to the LDL receptor at the cell surface. Upon reaching early endosomes, the LDL dis ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrolase
In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond: :\ce \quad \xrightarrowtext\quad \ce This typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases. Esterases cleave ester bonds in lipids and phosphatases cleave phosphate groups off molecules. An example of crucial esterase is acetylcholine esterase, which assists in transforming the neuron impulse into the acetate group after the hydrolase breaks the acetylcholine into choline and acetic acid. Acetic acid is an important metabolite in the body and a critical intermediate for other reactions such as glycolysis. Lipases hydrolyze glycerides. Glycosidases cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds. Nucleosidases hydrolyze the bonds of nucleo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Epsin
Epsins are a family of highly conserved membrane proteins that are important in creating membrane curvature. Epsins contribute to membrane deformations like endocytosis, and block vesicle formation during mitosis. Structure Epsin contains various protein domains that aid in function. Starting at the N-terminus is the ENTH domain. ENTH stands for Epsin N-Terminal Homolog. The ENTH domain is approximately 150 amino acids long and is highly conserved across species. It is composed of seven α-helices and an eighth helix that is not aligned with the seven helices that make up a superhelical fold. The role of the ENTH domain is to bind membrane lipids which is currently thought to aid in the invagination of the plasma membrane to form clathrin-coated vesicles. Additionally, located toward the C-terminus of the ENTH domain are two to three ubiquitin interacting motifs which aids in ubiquitin dependent recruitment. Following the ENTH domain there is not as much conservation in stru ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
