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BET11 and 12 are required for pollen tube elongation. Pollen tubes are rapidly growing specialized structures that elongate in a polar manner. They play a crucial role in the delivery of sperm cells through the stylar tissues of the flower and into the embryo sac, where the sperm cells are released to fuse with the egg cell and the central cell to give rise to the embryo and the endosperm. Polar growth at the pollen tube tip is believed to result from secretion of materials by membrane trafficking mechanisms. In this study, we report the functional characterization of Arabidopsis BET11 and BET12, two genes that may code for Qc-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors). Double mutants (bet11/bet12) in a homozygous/heterozygous background showed reduced transmission of the mutant alleles, reduced fertilization of seeds, defective embryo development, reduced pollen tube lengths and formation of secondary pollen tubes. Both BET11 and BET12 are required for fertility and development of pollen tubes in Arabidopsis. More experiments are required to dissect the mechanisms involved.
Rab GTPases, their effectors, SNAREs of the R, Qa, Qb, and Qc families, and SM SNARE-binding proteins catalyze intracellular membrane fusion. At the vacuole/lysosome, they are integrated by the homotypic fusion and vacuole protein sorting (HOPS) complex. Two HOPS subunits bind vacuolar Rabs for tethering, another binds the Qc SNARE, and a fourth HOPS subunit, an SM protein, has conserved grooves that bind R- and Qa-SNARE domains. Spontaneous quaternary SNARE complex assembly is very slow. We report an assay of SNARE complex assembly that does not rely on fusion and for which tethering does not coenrich the four SNAREs. HOPS is required in this assay for rapid SNARE complex assembly. Optimal assembly needs HOPS, lipid membranes to which the R- or Qa-SNARE and Ypt7:GTP are integrally bound, and each of the other three SNAREs. Each SNARE assembles into this complex relying on the others, suggesting four-SNARE complex assembly rather than direct binding of each to HOPS. SNAREs can be disassociated by Sec 17/Sec 18/ATP, completing a catalyzed cycle of SNARE assembly and disassembly.
SYP51 and 52 are the two members of the SYP5 Qc-SNARE gene family in Arabidopsis thaliana. These two proteins, besides their high level of sequence identity (85%), have shown to have differential functional specificity and possess a different interactome. Here we describe a unique and specific interaction of SYP51 with an ER aquaporin, AtNIP1;1 (also known as NLM1) indicated to be able to transport arsenite [As(III)] and previously localized on PM. In the present work we investigate in detail such localization in vivo and characterize the interaction with SYP51. We suggest that this interaction may reveal a new mechanism regulating tonoplast invagination and recycling. We propose this interaction to be part of a regulatory mechanism associated with direct membrane transport from ER to tonoplast and Golgi mediated vesicle trafficking. We also demonstrate that NIP1;1 is important for plant tolerance to arsenite but does not alter its uptake or translocation. To explain such phenomenon the hypothesis that SYP51/NIP1;1 interaction modifies ER and vacuole ability to accumulate arsenite is discussed.
Soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) proteins mediate membrane fusion and deliver cargo to specific cellular locations through vesicle trafficking. Synaptosome-associated protein of 25 kDa (SNAP25) is a target membrane SNARE that drives exocytosis by fusing plasma and vesicular membranes. In this study, we isolated GhSNAP33, a gene from cotton (Gossypium hirsutum), encoding a SNAP25-type protein containing glutamine (Q)b- and Qc-SNARE motifs connected by a linker. GhSNAP33 expression was induced by H2O2, salicylic acid, abscisic acid, and polyethylene glycol 6000 treatment and Verticillium dahliae inoculation. Ectopic expression of GhSNAP33 enhanced the tolerance of yeast cells to oxidative and osmotic stresses. Virus-induced gene silencing of GhSNAP33 induced spontaneous cell death and reactive oxygen species accumulation in true leaves at a later stage of cotton development. GhSNAP33-deficient cotton was susceptible to V. dahliae infection, which resulted in severe wilt on leaves, an elevated disease index, enhanced vascular browning and thylose accumulation. Conversely, Arabidopsis plants overexpressing GhSNAP33 showed significant resistance to V. dahliae, with reduced disease index and fungal biomass and elevated expression of PR1 and PR5. Leaves from GhSNAP33-transgenic plants showed increased callose deposition and reduced mycelia growth. Moreover, GhSNAP33 overexpression enhanced drought tolerance in Arabidopsis, accompanied with reduced water loss rate and enhanced expression of DERB2A and RD29A during dehydration. Thus, GhSNAP33 positively mediates plant defense against stress conditions and V. dahliae infection, rendering it a candidate for the generation of stress-resistant engineered cotton.
In flowering plants, hydration of desiccated pollen grains on stigma is a prerequisite for pollen germination, during which pollen increase markedly in volume through water uptake, requiring them to survive hypoosmotic shock to maintain cellular integrity. However, the mechanisms behind the adaptation of pollen to this hypoosmotic challenge are largely unknown. Here, we identify the Qc-SNARE protein SYP72, which is specifically expressed in male gametophytes, as a critical regulator of pollen survival upon hypoosmotic shock during hydration. SYP72 interacts with the MSCS-LIKE 8 (MSL8) and is required for its localization to the plasma membrane. Intraspecies and interspecies genetic complementation experiments reveal that SYP72 paralogs and orthologs from green algae to angiosperms display conserved molecular functions and rescue the defects of Arabidopsis syp72 mutant pollen facing hypoosmotic shock following hydration. Our findings demonstrate a critical role for SYP72 in pollen resistance to hypoosmotic shock through the MSL8 cascade during pollen hydration.
SNARE proteins are essential to vesicle trafficking and membrane fusion in eukaryotic cells. In addition, the SNARE-mediated secretory pathway can deliver diverse defense products to infection sites during exocytosis-associated immune responses in plants. In this study, a novel gene (CkSNAP33) encoding a synaptosomal-associated protein was isolated from Cynanchum komarovii and characterized. CkSNAP33 contains Qb- and Qc-SNARE domains in the N- and C-terminal regions, respectively, and shares high sequence identity with AtSNAP33 from Arabidopsis. CkSNAP33 expression was induced by H2O2, salicylic acid (SA), Verticillium dahliae, and wounding. Arabidopsis lines overexpressing CkSNAP33 had longer primary roots and larger seedlings than the wild type (WT). Transgenic Arabidopsis lines showed significantly enhanced resistance to V. dahliae, and displayed reductions in disease index and fungal biomass, and also showed elevated expression of PR1 and PR5. The leaves of transgenic plants infected with V. dahliae showed strong callose deposition and cell death that hindered the penetration and spread of the fungus at the infection site. Taken together, these results suggest that CkSNAP33 is involved in the defense response against V. dahliae and enhanced disease resistance in Arabidopsis.
Platelet secretion not only drives thrombosis and hemostasis, but also mediates a variety of other physiological and pathological processes. The ubiquitous SNARE machinery and a number of accessory proteins have been implicated in regulating secretion in platelet. Although several platelet SNAREs have been identified, further members of the SNARE family may be needed to fine-tune platelet secretion. In this study we identified expression of the t-SNARE syntaxin 8 (STX8) (Qc SNARE) in mouse and human platelets. In mouse studies, whereas STX8 was not essential for α-granule or lysosome secretion, Stx8(-/-) platelets showed a significant defect in dense granule secretion in response to thrombin and CRP. This was most pronounced at intermediate concentrations of agonists. They also showed an aggregation defect that could be rescued with exogenous ADP and increased embolization in Stx8(-/-) mice in vivo consistent with an important autocrine and paracrine role for ADP in aggregation and thrombus stabilization. STX8 therefore specifically contributes to dense granule secretion and represents another member of a growing family of genes that play distinct roles in regulating granule release from platelets and thus platelet function in thrombosis and hemostasis.
Neuronal morphogenesis involves dramatic plasma membrane expansion, fueled by soluble N-ethylmaleimide-sensitive factor attachment protein eceptors (SNARE)-mediated exocytosis. Distinct fusion modes described at synapses include full-vesicle fusion (FVF) and kiss-and-run fusion (KNR). During FVF, lumenal cargo is secreted and vesicle membrane incorporates into the plasma membrane. During KNR, a transient fusion pore secretes cargo but closes without membrane addition. In contrast, fusion modes are not described in developing neurons. Here, we resolve individual exocytic events in developing murine cortical neurons and use classification tools to identify four distinguishable fusion modes: two FVF-like modes that insert membrane material and two KNR-like modes that do not. Discrete fluorescence profiles suggest distinct behavior of the fusion pore. Simulations and experiments agree that FVF-like exocytosis provides sufficient membrane material for morphogenesis. We find the E3 ubiquitin ligase TRIM67 promotes FVF-like exocytosis in part by limiting incorporation of the Qb/Qc SNARE SNAP47 into SNARE complexes and, thus, SNAP47 involvement in exocytosis.
Vesicular trafficking is a fundamental cellular process involved in material transport in eukaryotes, but the diversity of the intracellular compartments has prevented researchers from obtaining a clear understanding of the specific functions of vesicular trafficking factors, including SNAREs, tethers, and Rab GTPases, in Apicomplexa. In this study, we analyzed the localization of SNAREs and investigated their roles in vesicular trafficking in Toxoplasma gondii. Our results revealed the specific localizations of SNAREs in the endoplasmic reticulum (ER) (T. gondii Stx18 [TgStx18] and TgStx19), Golgi stacks (TgGS27), and endosome-like compartment (TgStx10 and TgStx12). The conditional ablation of ER- and Golgi-residing SNAREs caused severe defects in the secretory system. Most importantly, we found an R-SNARE (TgVAMP4-2) that is targeted to the apicoplast; to our knowledge, this work provides the first information showing a SNARE protein on endosymbiotic organelles and functioning in vesicular trafficking in eukaryotes. Conditional knockout of TgVAMP4-2 blocked the entrance of TgCPN60, TgACP, TgATrx2, and TgATrx1 into the apicoplast and interfered with the targeting of TgAPT1 and TgFtsH1 to the outermost membrane of the apicoplast. Together, our findings revealed the functions of SNAREs in the secretory system and the transport of nucleus-encoded proteins to an endosymbiotic organelle in a model organism of Apicomplexa. IMPORTANCE SNAREs are essential for the fusion of the transport vesicles and target membranes and, thus, provide perfect targets for obtaining a global view of the vesicle transport system. In this study, we report that a novel Qc-SNARE (TgStx19) instead of Use1 is located at the ER and acts as a partner of TgStx18 in T. gondii. TgGS27 and the tethering complex TRAPP III are conserved and critical for the biogenesis of the Golgi complex in T. gondii. A novel R-SNARE, TgVAMP4-2, is found on the outermost membrane of the apicoplast. The transport of NEAT proteins into the secondary endosymbiotic organelle depends on its function. To our knowledge, this work provides the first mention of a SNARE located on endosymbiotic organelles that functions in vesicular trafficking in eukaryotes.
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