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4 edition of Search for targeting sequences in the synthetic vesicle membrane protein, VAMP-2 found in the catalog.

Search for targeting sequences in the synthetic vesicle membrane protein, VAMP-2

Mahmood Mohtashami

Search for targeting sequences in the synthetic vesicle membrane protein, VAMP-2

by Mahmood Mohtashami

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Published by National Library of Canada in Ottawa .
Written in English


Edition Notes

Thesis (M.Sc.)--University of Toronto, 1993.

SeriesCanadian theses = Thèses canadiennes
The Physical Object
FormatMicroform
Pagination1 microfiche : negative.
ID Numbers
Open LibraryOL15478942M
ISBN 100315924470
OCLC/WorldCa35945193

In some proteins the only transmembrane sequence is located C-terminally in the protein. These proteins are recognized by The major model of vesicle fusion holds that actual fusion of a vesicle with its target membrane is driven by the interaction of pairs of proteins called vesicle and target. A patient was diagnosed to possess a mutation in an ER-resident protein in which the ER-signal sequences of the protein were inappropriately deleted and instead replaced with a mannosephosphate during protein synthesis and posttranslational modification. What is the likely fate of this mutant protein? The protein never enters the Golgi complex.

A clue to understand such membrane protein sorting was obtained from our work on the Rer1p-dependent localization of ER membrane proteins. Rer1p is a Golgi-resident membrane protein of amino acid residues containing four membrane-spanning domains and is required for the ER localization of the type-II membrane protein Sec12p (Nishikawa and. VAMP cleavage abolishes the interaction with the adaptor protein AP3 and affects synaptic vesicle recycling via early endosomes [].The SNARE cleavage products have also the potential to interfere with fusion processes [,].Consistent with synaptophysin-1 controlling specifically the targeting of VAMP2 (but not VAMP1) to synaptic vesicles is the observation that the cytosolic cleavage.

However, it is not the coat proteins that determine the target of a transport vesicle; instead, this is the role of proteins called SNAREs, which separately reside on the vesicle and target membranes. Together, the coat proteins and the SNAREs coordinate the trafficking of the cargo between the various organelles of the endomembrane system. The vesicle associated membrane proteins (VAMP) or synaptobrevins are calcium binding proteins specific to eukaryotes. VAMPs, along with synaptosomal associated protein of 25 kDa (SNAP) and syntaxin, form the core complex of soluble NSF attachment protein receptor (SNARE) proteins that interact with the soluble proteins N-ethylmaleimide.


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Search for targeting sequences in the synthetic vesicle membrane protein, VAMP-2 by Mahmood Mohtashami Download PDF EPUB FB2

Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles (By similarity.

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 ro: IPR   Non-technical summary.

Mucin secretion in the lung is regulated by the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) exocytotic core, which has not been defined in airway goblet this study, the SNARE vesicle-associated membrane protein 8 (VAMP8) was found to be expressed in human airway epithelial goblet by: Validating this approach was our key observation that synthetic peptides corresponding to functional signal sequences inhibit the translocation of precursor proteins across E.

coli membrane vesicles, while nonfunctional peptides do not. 29 The inhibition seemed to be protein-mediated, and could be reversed, at least in part, by addition of an Cited by: The delivery of secretory vesicles to appropriate docking and fusion sites on the plasma membrane is crucial for many cellular functions, including formation of synapses, exocytosis of neurotransmitter, establishment and maintenance of cell polarity, cell growth and plasma membrane wound healing.

Cell-biological, genetic and biochemical approaches have identified crucial proteins and protein Cited by: In rice (Oryza sativa) endosperm cells, mRNAs encoding glutelin and prolamine are translated on distinct cortical-endoplasmic reticulum (ER) subdomains (the cisternal-ER and protein body-ER), a process that facilitates targeting of their proteins to different endomembrane compartments.

Although the cis - and trans -factors responsible for mRNA localization have been defined over the years. Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system.

J Biol Chem. Jul 5; (19)– Matthew WD, Tsavaler L, Reichardt LF. Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue.

Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins play key roles in membrane fusion, but their sorting to specific membranes is poorly er, individual SNARE proteins can function in multiple membrane fusion events dependent upon their trafficking itinerary.

Synaptosome-associated protein of 25 kDa (SNAP25) is a plasma membrane Q (containing. Protein knowledgebase. UniParc. Sequence archive. Help. Help pages, FAQs, UniProtKB manual, documents, news archive and Biocuration projects.

UniRef. Sequence clusters. Proteomes. Protein sets from fully sequenced genomes. Annotation systems.

Systems used to automatically annotate proteins with high accuracy: UniRule (Expertly curated rules). Gavel, Y., and von Heijne, G.,The distribution of charged amino acids in mitochondrial inner membrane proteins suggests different modes of membrane integration for nuclearly and mito-chondrially encoded proteins, Eur.

Biochem. –   The VAMPs are included among a complex of proteins known as SNAREs that serve as a receptor for two proteins, SNAP and NSF, required for vesicle-mediated transport (Sollner et al., ).

VAMPs are located on transport vesicles and bind to a protein member of the syntaxin family present in the target membrane (Calakos et al., ).

Search for courses, skills, and videos. Main content. Science Biology library Central dogma (DNA to RNA to protein) Translation. Protein targeting. How molecular labels are used to direct proteins to different parts of the cell (and to the cell exterior).

Google Classroom Facebook Twitter. Email. Background. Intracellular vesicle fusion is mediated by the interactions of SNARE (s oluble N-ethylmaleimide-sensitive factor a ttachment protein re ceptor) proteins on vesicles (v-SNAREs) and on target membranes (t-SNAREs).The vesicle-associated membrane proteins (VAMPs) are v-SNAREs that reside in various post-Golgi vesicular compartments.

BoNT/FA cleaves the same intracellular target proteins as BoNT/F1 and other F serotype BoNTs; the intracellular targets are vesicle associated membrane proteins (VAMP) 1, 2 and 3.

BoNT/FA cleaves the same site in VAMP-2 as BoNT/F5, which is different from the cleavage site of other F serotype BoNTs. A 42K outer-membrane protein is a component of the yeast mitochondrial protein import site. NatureCrossref, Medline, Google Scholar; 42 Walter P., Johnson A.E.

Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell. Biol. 10, Crossref, Medline, Google Scholar. two different N-terminal targeting sequences (both ultimately cleaved: two protease): matrix-targeting sequence and Intermembrane -space-targeting sequence 2.

No N-terminal matrix-targeting sequence-delivered directly to the inter membrane space-folding and disulfide bond formation which irreversibly traps the protein in the intermembrane space. Carrier-protein conjugated synthetic peptide encompassing a sequence within the N-terminus region of mouse VAMP2.

The exact sequence is proprietary. vesicle-associated membrane protein 2, Syb-2, Syb2, Vamp-2, sybII Background Involved in the targeting and/or fusion of transport vesicles to their target membrane. In neuronal cells, the hypothesis is proposed that synaptic vesicles dock to a target membrane through the interaction of vesicular and target membrane proteins referred to as SNAP receptors (SNAREs) (11, 12).

VAMP-2 is a vesicle-docked SNARE (v-SNARE), and syntaxin1 and SNAP are target membrane SNAREs (t-SNAREs). Vesicle-associated membrane protein 7 (VAMP-7) is essential for target cell killing in a natural killer cell line Author links open overlay panel Marcelo Marcet-Palacios a Solomon O.

Odemuyiwa a Jason J. Coughlin a Daniella Garofoli a Catherine Ewen b Courtney E. Davidson a Mazyar Ghaffari a Kevin P.

Kane c Paige Lacy a Michael R. Logan a A. K.T. Rognlien, D.J. Woodbury, in Membrane Science and Technology, 1 INTRODUCTION. SNARE proteins are molecular motors that drive the biological fusion of two membranes [1].Part of the motor assembly is in the vesicle membrane (v-SNAREs) and part is in the target membrane (t-SNAREs) [2,3].During fusion many matched pairs of v- and t-SNAREs intertwine to pull opposing.

theelectromotornucleus. OnecloneencodesVAMP-1(vesicle-associated membrane protein 1), a nervous-system-specific protein of amino acids whose primary sequence can be divided into three domains: aproline-rich aminoterminus, a highly charged internal region, andahydrophobic carboxyl-terminal domain that is predicted to comprise a membrane anchor.Vesicle-associated membrane protein 2 (VAMP2 or synaptobrevin 2) has been shown to be the predominant v-SNARE that targets small synaptic vesicles (SSVs) to the presynaptic plasma membrane by interacting with its cognate t-SNAREs, syntaxin 1 and synaptosome-associated protein of 25 kDa (SNAP) found on the target membrane (reviewed in Refs.Vesicle-associated membrane protein (VAMP), also known as synaptobrevin, is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicles.

Two VAMP homologs, VAMP1 and VAMP2, are differentially expressed in the nervous system.