Abstract
Plants comprise an expanded endomembrane system, and transport within the network requires well-organized and accurate vesicle transport. Tethering complexes facilitate the early, exact contact among donor and acceptor membranes, operate to bring vesicles into a closer proximity for trans-SNARE complex assembly docking; these are classified as either long coiled-coil proteins or multi-subunit tethering complexes (MTCs). Numerous MTCs that function at different membrane trafficking steps have been recognized, where they function as significant interfaces between SNARE proteins, Rabs, and phosphoinositides. SNARE proteins assemble into complexes that catalyze the fusion between a donor and a target membrane. Studies of the diverse SNARE proteins provided further valuable information about vacuole biogenesis and vacuolar trafficking pathways related to cell-type specificity, plant development, growth, and the plant developed a specific traffic route to overcome environmental stress. In conclusion, tethers' selective recruitment during membrane fusion is controlled via diverse small GTPases, such as those in the RAB family. The MTCs promote SNARE complex assembly by direct interactions of MTC subunits with Q-SNAREs. A subset of MTC subunits exploits structurally similar CATCHR domains to mediate inter-subunit interactions as well as SNARE protein interactions. MTCs are subdivided into CATCHR (complexes associated with tethering containing helical rods: Dsl1, COG, GARP, EARP, and exocyst) and non‐CATCHR (TRAPP I, II and III, HOPS and CORVET) complexes based on the structure of their subunits. This review summarized new information about SNARE proteins and tethering complexes, highlight new insights about their function, and discuss current debates and future perspectives.
Highlights
1-All about Soluble N-ethylmaleimidesensitive factor attachment protein receptor (SNARE): SNARE small molecule protein composed of 100-300 amino acids
SNARE proteins can be divided into two categories depending on the positioning: V-SNARE positioned on the transport vesicles and t-SNARE positioned on the target membrane
A typical SNARE complex consists of Qa-(syntaxin1 positioned on the target membrane-like), Qb-(N-terminal half of SNAP25 like), Qc(C-terminal half of SNAP25 like) SNARE, and R-SNARE (VAMP/synaptobrevin) on the donor membrane composition (Hong & Lev, 2014)
Summary
Vacuole in Plants: In plant cells, vacuoles are vital organelles that sustain cellular homeostasis, serving as reservoirs for numerous molecules and function as lytic organelles to break down and recycle cellular components. AtVps mutations disrupted pollen tubes' diffusion into the transmitting tissue, leading to failed male transmission; multiple small vacuoles were detected in the AtVps pollen tubes This phenotype is more severe than that in the vcl pollen tube, suggesting that the AtVps subunit might play some functions independent of the HOPS-core subunits (Tan, Wei, Li, Wang, & Bao, 2017). The other unit covers RAB7, HOPS, and the VAMP71 containing the SNARE complex This unit facilitates homotypic fusion among vacuoles, considering the colocalization of HOPS components and VAMP71 at the interaction sites among vacuoles and the fragmented vacuole phenotype brought via depletion of VAMP71 or HOPS components. 6-Conclusion This review discussed that SNARE proteins play very important roles in plant development; SNAREs have a central role in vesicle traffic via driving membrane fusion and conferring fidelity via forming specific SNARE complexes.
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