2 edition of Studying the roles of drosophila snares in membrane traffic. found in the catalog.
Studying the roles of drosophila snares in membrane traffic.
Written in English
Thesis (Ph.D.) -- University of Toronto, 2003.
|The Physical Object|
|Number of Pages||241|
A few membrane vesicle trafficking (SNARE) proteins in plants are associated with signaling and transmembrane ion transport, including control of plasma membrane ion channels. Vesicle traffic contributes to the population of ion channels at the plasma membrane. Nonetheless, it is unclear whether these SNAREs also interact directly to affect channel gating and, if so, what functional impact. SNAREs are important for membrane homophilic fusion during autophagosome formation (17, 46). Sec22 facilitates Atg9 recruitment to the phagophore assembly site and therefore is required for autophagosome formation in yeast. However, in our study, Sec22 was dispensable for starvation-induced autophagy in flies.
The phenotypic differences are most apparent when the phenotypes are compared in the same organ, the well described retina of Drosophila. The ubiquitous distribution of Syb (20, 21) had predicted a role in general cellular traffic to the membrane surface, and consistent with this hypothesis, the absence of Syb proved lethal to the homozygous cells. These experiments suggest that in Drosophila, Damph functions during SNARE-dependent postsynaptic FasII membrane cycling. This study challenges the notion that synaptic Amphiphysin is involved exclusively in endocytosis and suggests a novel role for this protein in postsynaptic exocytosis.
SNARE proteins are classified by the Q or R amino acid residue found at the core of the interacting assembly and localize to vesicle (R-SNAREs or vesicle-associated membrane proteins [VAMPs]) and target (Qa-, Qb-, and Qc-SNAREs) membranes (Fasshauer et al., ; Blatt and Thiel, ; Jahn and Scheller, ).SNARE function is conserved within eukaryotes, but these gene families are similarly. The directed traffic of membrane proteins to the cell surface is crucial for many developmental events. We describe the role of Sec5, a member of the exocyst complex, in directed membrane traffic in the Drosophila oocyte. During oogenesis, we find that Sec5 localization undergoes dynamic changes, correlating with the sites at which it is required for the traffic of membrane proteins.
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To distinguish the unique function of each SNAP related molecule in membrane traffic, binding partners beyond the SNARE super-family are being identified and studied. To-date, mammalian SNAP has been shown to interact with SNIP (SNAPinteracting protein), Hrs (hepatocyte growth factor-regulated tyrosine kinase substrate), and by: Indeed, many cells differ greatly in subcellular organization and secretory function, and the Drosophila system provides an excellent model to understand how this diversity is established.
Many proteins known to play important roles in membrane trafficking are conserved in Drosophila (Schlacht et al., ; Zhang et al., ).Cited by: The SNARE Hypothesis According to this hypothesis, SNAPs bind to their receptors SNARES on the vesicle (v-SNARE) and the target membrane (t-SNARE).
NSF then binds to SNAPs, and, in the presence of other hitherto uncharacterized cytoplasmic and membrane proteins, the interaction between two membranes is potentiated that ultimately leads to their Cited by: SNAREs (SNAP receptors) are the key components of protein complexes that drive membrane fusion.
Here, we report the function of a SNARE, Syntaxin 5 (Syx5), in the development of photoreceptors in Drosophila. In wild type photoreceptors, Syx5 localizes to cisi,-Golg along with cis-Golgi markers, Rab1, and GM We observed thatCited by: Epithelial cells have an apical–basolateral axis of polarity, which is required for epithelial functions including barrier formation, vectorial ion transport and sensory perception.
Here we Cited by: The observations indicated a role for Studying the roles of drosophila snares in membrane traffic. book Q-SNARE in traffic to the plasma membrane. They also raised questions about additional functions in regulating ion channel activities, either through selective exocytosis and endocytosis of the channel proteins or through direct signaling associations and regulation within the plane of the membrane.
The role of membrane traffic as a driving force for cytokinesis was abandoned after the discovery of the actin ring but was resurrected later (see below). In higher plant cells, which have no myosin II and no contractile cortex, the importance of membrane traffic was recognized a century ago.
SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) are now generally accepted to be the major players in the final stage of the docking and the subsequent fusion of diverse vesicle-mediated transport SNARE-mediated process is conserved evolutionally from yeast to human, as well as mechanistically and structurally across different.
This book details multiple ways that soluble N-ethylmaleimide-sensitive factor attachment protein receptors(SNAREs) and their function are examined in the methods described in each chapter are described in detail so that novice as well as experienced researchers can explore the mechanisms of SNARE-mediated membrane fusion.
Tetanus neurotoxin-insensitive vesicle-associated membrane protein (TI-VAMP) is a vesicle-SNARE (soluble N-ethylmaleimide-sensitive fusion protein [NSF] attachment protein [SNAP] receptor), involved in transport to the apical plasma membrane in epithelial cells, a tetanus neurotoxin-resistant pathway.
Here we show that TI-VAMP is essential for. SNAREs are located on plasma membrane, lysosomes/vacuoles, Golgi membranes, endoplasmic reticulum, and the vesicles derived from each of these membranes [15,16]. Sec22 is an important R-SNARE involved in membrane fusion in Eukaryotes.
Sec22 localizes to ER and Golgi and helps in anterograde and retrograde transport of vesicles [17,18,19]. SNARE isoforms appear to regulate specific intracellular membrane trafficking steps. To identify new SNARE proteins in Drosophila melanogaster we used a yeast two-hybrid screen to search for proteins that interact with SNAP.
Here we report the identification of the Drosophila homologue of syntaxin dsyntaxin 16 binds SNAP in a concentration-dependent fashion and genetically interacts with NSF2.
SNAREs (SNAP receptors) are the key components of protein complexes that drive membrane fusion. Here, we report the function of a SNARE, Syntaxin 5 (Syx5), in the development of photoreceptors in Drosophila.
In wild-type photoreceptors, Syx5 localizes to cis- Golgi, along with cis- Golgi markers: Rab1 and GM We observed that Syx5-deficient photoreceptors show notable accumulation of.
among the most important and widely studied proteins in membrane trafficking, docking, and fusion are the soluble N-ethylmaleimide-sensitive factor activating protein receptors, or proteins are membrane-associated proteins that contain characteristic SNARE domains: heptad repeats ∼60 amino acids in length that are predicted to form coiled-coils.
A second strategy, making use of dominant negative inhibitors complementary to a selected SNARE, was first employed by Leyman et al.
() to explore the role for the tobacco SNARE NtSYP in K + and Cl − channel control and was subsequently used to examine the functioning of the same SNARE in membrane vesicle traffic and development. components of the membrane fusion apparatus that may be involved and point to possible roles for an emer-ging family of cytoskeletal proteins, the septins, in this process.
Key words: Abscission, actomyosin, cleavage furrow, contractile ring, cytokinesis, membrane traffic, micro-tubules, midbody, septin, SNAREs, vesicle fusion. Despite the recent progress in the field of membrane traffic, the question of how the specificity of membrane fusion is achieved has yet to be resolved.
It has become apparent that the SNARE proteins, although central to the process of fusion, are often not the first point of contact between a vesicle and its target. Instead, a poorly understood tethering process physically links the two.
Roles of ZW10, Rod and Rint1 in Drosophila membrane trafficking. Our cytological and phenotypic analyses demonstrate for the first time that Zw10 plays a role in Drosophila membrane traffic. During male meiosis Zw10 is enriched both at the Golgi stacks and at ER structures such as the spindle envelope and the astral membranes.
Abstract. SNAP is expressed throughout the life cycle of fruit fly and exhibits wide tissue distribution patterns. Unlike other SNAPlike proteins (i.e., SNAP, SNAP/24, and SNAP) which primarily support exocytosis at the plasma membrane, SNAP regulates various intracellular trafficking events, by partnering with proteins active in both exocytosis and endocytosis.
SNAREs participate actively to accommodate membrane fusion in regulated pathways in at least two ways. In mast cells, the t-SNARE component SNAP23 is relocated to granule membranes to allow for membrane fusion during compound exocytosis.
Our present results now show a second and distinct role for SNAREs, which increase in abundance at the. Each membrane fusion event along the secretory and endocytic pathways requires a specific set of SNAREs to assemble into a 4-helical coiled-coil, the so-called trans-SNARE complex.
Although most SNAREs contribute one helix to the trans-SNARE complex, members of the SNAP family contribute two helixes. We report the characterization of the Drosophila homologue of SNAP. Levels of membrane-surface FasII are decreased in damph mutants. To study the function of Damph at Drosophila synapses, we used the third-instar larval NMJ, a powerful model system to study glutamatergic synapse development and function.
At these synapses, Damph localizes primarily at the postsynaptic region in colocalization with a number of synaptic proteins, including.
SNAREs have recently been shown to regulate autophagosome formation in both mammalian cells and in ye In mammalian cells, the SNAREs vesicle-associated membrane protein (VAMP)7, syntaxin-7, syntaxin-8, and VTI1B regulate the homotypic fusion of phagophore precurs These fusion events enable the growth of these structures into a tubular network .