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Synaptobrevin
Synaptobrevins (''synaptobrevin isotypes 1-2'') are small integral membrane proteins of secretory vesicles with molecular weight of 18 kilodalton (kDa) that are part of the vesicle-associated membrane protein (VAMP) family. Synaptobrevin is one of the SNARE proteins involved in formation of the SNARE complexes. Structure Out of four α-helices of the core SNARE complex one is contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 (in neurons). Function SNARE proteins are the key components of the molecular machinery that drives fusion of membranes in exocytosis. Their function however is subject to fine-tuning by various regulatory proteins collectively referred to as ''SNARE masters''. Classification In the Q/R nomenclature for organizing SNARE proteins, VAMP/synaptobrevin family members are classified as R-SNAREs, so named for the presence of an arginine at a specific location within the primary sequence of the protein (as opposed to the SNAREs of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Q-SNARE
SNARE proteins – " SNAP REceptor" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate vesicle fusion – the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments (such as a lysosome). The best studied SNAREs are those that mediate the neurotransmitter release of synaptic vesicles in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria. Types SNAREs can be divided into two categories: ''vesicle'' or ''v-SNAREs'', which are incorporated into the membranes of transport vesicles during budding, and ''target'' or ''t-SNAREs'', which are associated with nerve terminal membranes. Evidence suggests that t-SNAREs form stable subcomplexes which serve as guides ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SNARE Proteins
SNARE proteins – " SNAP REceptor" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate vesicle fusion – the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments (such as a lysosome). The best studied SNAREs are those that mediate the neurotransmitter release of synaptic vesicles in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria. Types SNAREs can be divided into two categories: ''vesicle'' or ''v-SNAREs'', which are incorporated into the membranes of transport vesicles during budding, and ''target'' or ''t-SNAREs'', which are associated with nerve terminal membranes. Evidence suggests that t-SNAREs form stable subcomplexes which serve as guides ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
R-SNAREs
SNARE proteins – " SNAP REceptor" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate vesicle fusion – the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments (such as a lysosome). The best studied SNAREs are those that mediate the neurotransmitter release of synaptic vesicles in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria. Types SNAREs can be divided into two categories: ''vesicle'' or ''v-SNAREs'', which are incorporated into the membranes of transport vesicles during budding, and ''target'' or ''t-SNAREs'', which are associated with nerve terminal membranes. Evidence suggests that t-SNAREs form stable subcomplexes which serve as guid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
VAMP2
Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the ''VAMP2'' gene. Function Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP2 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. VAMP2 is thought to participate in neurotransmitter release at a step between docking and fusion. Mice lacking functional synaptobrevin2/VAMP2 gene cannot survive after birth, and have a dramatically reduced synaptic transmission, around 10% of control. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and complexin. It also forms a distinct complex with synaptophysin. Clinical significance Heterozygous mutations in VAMP2 cause a neurodevelopmental disorder with hypotonia and autistic features (with or with ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SNAP-25
Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (''N''-ethylmaleimide-sensitive factor) Attachment Protein Receptor (t-SNARE) protein encoded by the ''SNAP25'' gene found on chromosome 20p12.2 in humans. SNAP-25 is a component of the ''trans''-SNARE complex, which accounts for membrane fusion specificity and directly executes fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together. Structure and function SNAP-25, a Q-SNARE protein, is anchored to the cytosolic face of membranes via palmitoyl side chains covalently bound to cysteine amino acid residues in the central linker domain of the molecule. This means that SNAP-25 does not contain a trans-membrane domain. SNAP-25 has been identified to contribute two α-helices to the SNARE complex, a four-α-helix domain complex. The SNARE complex participates in vesicle fusion, which involves the docking, priming and merging of a vesicle with the cell membrane t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tetanospasmin
Tetanus toxin (TeNT) is an extremely potent neurotoxin produced by the vegetative cell of '' Clostridium tetani'' in anaerobic conditions, causing tetanus. It has no known function for clostridia in the soil environment where they are normally encountered. It is also called spasmogenic toxin, tentoxilysin, tetanospasmin or, tetanus neurotoxin. The LD50 of this toxin has been measured to be approximately 2.5–3 ng/kg, making it second only to the related botulinum toxin (LD50 2 ng/kg) as the deadliest toxin in the world. However, these tests are conducted solely on mice, which may react to the toxin differently from humans and other animals. ''C. tetani'' also produces the exotoxin tetanolysin, a hemolysin, that causes destruction of tissues. Distribution Tetanus toxin spreads through tissue spaces into the lymphatic and vascular systems. It enters the nervous system at the neuromuscular junctions and migrates through nerve trunks and into the central nervou ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
VAMP1
Vesicle-associated membrane protein 1 (VAMP1) is a protein that in humans is encoded by the ''VAMP1'' gene. Function Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP1 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Multiple alternative splice variants that encode proteins with alternative carboxy ends have been described, but the full-length nature of some variants has not been defined. Clinical significance Homozygous mutations in VAMP1 have been identified in a series of children affected with a form of congenital myasthenic syndrome Congenital myasthenic syndrome (CMS) is an inherited neuromuscular disorder caused by defects of several types at the neuromuscular junction. The effects of the disease are similar to Lambert-Eaton Syndrome and myasthenia gravis ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
VAMP5
''Vesicle-associated membrane protein 5'' also known as ''VAMP5'' is a human gene which encodes a member of the synaptobrevin protein family. Function VAMPs (synaptobrevins) along with syntaxins and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of vesicles and cell membranes. The VAMP5 gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. This VAMP family member may participate in vesicle trafficking events that are associated with myogenesis Myogenesis is the formation of skeletal muscular tissue, particularly during embryonic development. Muscle fibers generally form through the fusion of precursor myoblasts into multinucleated fibers called ''myotubes''. In the early development .... References External links * {{gene-2-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SYBL1
Synaptobrevin-like protein 1 (SYBL1), also known as vesicle-associated membrane protein 7 (VAMP7), is a protein that in humans is encoded by the ''VAMP7'', or ''SYBL1'', gene. Function SYBL1 is a transmembrane protein that is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family. SYBL1 localizes to late endosomes and lysosome A lysosome () is a membrane-bound organelle found in many animal cells. They are spherical vesicles that contain hydrolytic enzymes that can break down many kinds of biomolecules. A lysosome has a specific composition, of both its membrane ...s and is involved in the fusion of transport vesicles to their target membranes. Interactions SYBL1 has been shown to interact with SNAP23 and AP3D1. References Further reading * * * * * * * * * * * * * * * * * External links * {{gene-X-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Syntaxin
Syntaxins are a family of membrane integrated Q-SNARE proteins participating in exocytosis. Domains Syntaxins possess a single C-terminal transmembrane domain, a SNARE domain (known as H3), and an N-terminal regulatory domain (Habc). Syntaxin 17 may have two transmembrane domains. * The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Formation of this stable SNARE core complex is believed to generate the free energy required to initiate fusion between the vesicle membrane and plasma membrane. * The N-terminal Habc domain is formed by 3 α-helices and when collapsed onto its own H3 helix forms an inactive "closed" syntaxin conformation. This closed conformation of syntaxin is believed to be stabilized by binding of Munc-18 (nSec1), although more recent data suggests that nSec1 may bind to other conformations of syntaxin, as well. The "open" syntaxin conformation is the conformation that is competent to form into SNARE core complexes. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vesicle-associated Membrane Protein
Vesicle associated membrane proteins (VAMP) are a family of SNARE proteins with similar structure, and are mostly involved in vesicle fusion. * VAMP1 and VAMP2 proteins known as synaptobrevins are expressed in brain and are constituents of the synaptic vesicles, where they participate in neurotransmitter release. * VAMP3 (known as cellubrevin) is ubiquitously expressed and participates in regulated and constitutive exocytosis as a constituent of secretory granules and secretory vesicles. * VAMP5 and VAMP7 (SYBL1) participate in constitutive exocytosis. ** VAMP5 is a constituent of secretory vesicles, myotubes and tubulovesicular structures. ** VAMP7 is found both in secretory granules and endosomes. * VAMP8 (known as endobrevin) participates in endocytosis Endocytosis is a cellular process in which 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 containin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Exocytosis
Exocytosis () is a form of active transport and bulk transport in which a cell transports molecules (e.g., neurotransmitters and proteins) out of the cell ('' exo-'' + '' cytosis''). As an active transport mechanism, exocytosis requires the use of energy to transport material. Exocytosis and its counterpart, endocytosis, are used by all cells because most chemical substances important to them are large polar molecules that cannot pass through the hydrophobic portion of the cell membrane by passive means. Exocytosis is the process by which a large amount of molecules are released; thus it is a form of bulk transport. Exocytosis occurs via secretory portals at the cell plasma membrane called porosomes. Porosomes are permanent cup-shaped lipoprotein structure at the cell plasma membrane, where secretory vesicles transiently dock and fuse to release intra-vesicular contents from the cell. In exocytosis, membrane-bound secretory vesicles are carried to the cell membrane, where ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
