Biomaterial Database

Regulation of intracellular membrane interactions: recent progress in the field of neurotransmitter release. 1998

M M Burger, and T Schäfer

Friedrich Miescher-Institute, Basel, Switzerland. burger@fmi.ch

Maintenance of compartmental independence and diversity is part of the blueprint of the eukaryotic cell. The molecular composition of every organelle membrane is custom tailored to fulfill its unique tasks. It is retained by strict sorting and directional transport of newly synthesized cellular components by the use of specific transport vesicles. Temporally and spatially controlled membrane fission and fusion steps thus represent the basic process for delivery of both, membrane-bound and soluble components to their appropriate destination. This process is fundamental to cell growth, organelle inheritance during cell division, uptake and intracellular transport of membrane-bound and soluble molecules, and neuronal communication. The latter process has become one of the best studied examples in terms of regulatory mechanisms of membrane interactions. It has been dissected into the stages of transmitter vesicle docking, priming, and fusion: Specificity of membrane interactions depends on interactions between sets of organelle-specific membrane proteins. Priming of the secretory apparatus is an ATP-dependent process involving proteins and membrane phospholipids. Release of vesicle content is triggered by a rise in intracellular free Ca2+ levels that relieves a block previously established between the membranes poised to fuse. Neurotransmitter release is a paradigm of highly regulated intracellular membrane interaction and molecular mechanisms for this phenomenon begin to be delineated.

UI	MeSH Term	Description	Entries
D007425	Intracellular Membranes	Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.	Membranes, Intracellular,Intracellular Membrane,Membrane, Intracellular
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008954	Models, Biological	Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.	Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D050600	SNARE Proteins	A superfamily of small proteins which are involved in the MEMBRANE FUSION events, intracellular protein trafficking and secretory processes. They share a homologous SNARE motif. The SNARE proteins are divided into subfamilies: QA-SNARES; QB-SNARES; QC-SNARES; and R-SNARES. The formation of a SNARE complex (composed of one each of the four different types SNARE domains (Qa, Qb, Qc, and R)) mediates MEMBRANE FUSION. Following membrane fusion SNARE complexes are dissociated by the NSFs (N-ETHYLMALEIMIDE-SENSITIVE FACTORS), in conjunction with SOLUBLE NSF ATTACHMENT PROTEIN, i.e., SNAPs (no relation to SNAP 25.)	SNAP Receptor,SNARE Protein,NSF Attachment Protein Receptor,Receptor, SNAP,SNAP Receptors,SNARE,SNAREs,Soluble N-ethylmaleimide-Sensitive-Factor Attachment Protein Receptor,Target Membrane SNARE Proteins,Target SNARE Proteins,Vesicle SNARE Proteins,Vesicular SNARE Proteins,t-SNARE,tSNAREs,v-SNARE,v-SNAREs,Protein, SNARE,SNARE Proteins, Target,SNARE Proteins, Vesicle,SNARE Proteins, Vesicular,Soluble N ethylmaleimide Sensitive Factor Attachment Protein Receptor,v SNAREs
D018377	Neurotransmitter Agents	Substances used for their pharmacological actions on any aspect of neurotransmitter systems. Neurotransmitter agents include agonists, antagonists, degradation inhibitors, uptake inhibitors, depleters, precursors, and modulators of receptor function.	Nerve Transmitter Substance,Neurohormone,Neurohumor,Neurotransmitter Agent,Nerve Transmitter Substances,Neurohormones,Neurohumors,Neuromodulator,Neuromodulators,Neuroregulator,Neuroregulators,Neurotransmitter,Neurotransmitters,Substances, Nerve Transmitter,Transmitter Substances, Nerve,Substance, Nerve Transmitter,Transmitter Substance, Nerve
D033921	Vesicular Transport Proteins	A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.	Transport Proteins, Vesicular