BIOMAT Database Logo BIOMAT Database Logo

Selective activation of cognate SNAREpins by Sec1/Munc18 proteins. 2007

Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
Department of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA.

Sec1/Munc18 (SM) proteins are required for every step of intracellular membrane fusion, but their molecular mechanism of action has been unclear. In this work, we demonstrate a fundamental role of the SM protein: to act as a stimulatory subunit of its cognate SNARE fusion machinery. In a reconstituted system, mammalian SNARE pairs assemble between bilayers to drive a basal fusion reaction. Munc18-1/nSec1, a synaptic SM protein required for neurotransmitter release, strongly accelerates this reaction through direct contact with both t- and v-SNAREs. Munc18-1 accelerates fusion only for the cognate SNAREs for exocytosis, therefore enhancing fusion specificity.

UI MeSH Term Description Entries
D008561 Membrane Fusion The adherence and merging of cell membranes, intracellular membranes, or artificial membranes to each other or to viruses, parasites, or interstitial particles through a variety of chemical and physical processes. Fusion, Membrane,Fusions, Membrane,Membrane Fusions
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
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D009474 Neurons The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM. Nerve Cells,Cell, Nerve,Cells, Nerve,Nerve Cell,Neuron
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D005089 Exocytosis Cellular release of material within membrane-limited vesicles by fusion of the vesicles with the CELL MEMBRANE.
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
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

Related Publications

Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
SNARE zippering requires activation by SNARE-like peptides in Sec1/Munc18 proteins.
September 2018, Proceedings of the National Academy of Sciences of the United States of America,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
SNARE-ing the structures of Sec1/Munc18 proteins.
December 2014, Current opinion in structural biology,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
A role for Sec1/Munc18 proteins in platelet exocytosis.
August 2003, The Biochemical journal,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
Sec1/Munc18 proteins: mediators of membrane fusion moving to center stage.
August 2000, Neuron,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.
August 2013, Proceedings of the National Academy of Sciences of the United States of America,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
Convergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteins.
January 2003, Proceedings of the National Academy of Sciences of the United States of America,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
Selective expression of a sec1/munc18 member in sea urchin eggs and embryos.
October 2004, Gene expression patterns : GEP,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
The ZIP Code of Vesicle Trafficking in Apicomplexa: SEC1/Munc18 and SNARE Proteins.
October 2020, mBio,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
SEC-uring membrane fusion: a sneak peek at SNARE-complex assembly driven by Sec1-Munc18 proteins.
October 2015, Nature structural & molecular biology,
Jingshi Shen, and David C Tareste, and Fabienne Paumet, and James E Rothman, and Thomas J Melia
Functional Reconstitution of Intracellular Vesicle Fusion Using Purified SNAREs and Sec1/Munc18 (SM) Proteins.
January 2019, Methods in molecular biology (Clifton, N.J.),
Copied contents to your clipboard!