SNARE proteins and their role in plant ion channel regulation
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REVIEW PAPER
SNARE proteins and their role in plant ion channel regulation Ben Zhang1 · Hui Wang1 · Yaxian Zhang1 Received: 2 July 2020 / Accepted: 24 August 2020 © Springer Nature B.V. 2020
Abstract SNAREs (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors) perform the final membrane fusion step of membrane traffic in plant through forming a SNARE complex. Except for the canonical role of membrane fusion, SNAREs are involved in the regulation of subcellular trafficking of ion channels. Recent research has identified that SNAREs also affect ion channel activity through protein–protein interaction. Here, we focused on the role of SNAREs in plant biology, especially on the ion channel regulation, which will advance the knowledge of plant growth and development. Keywords SNARE · Ion channel · Protein–protein interaction · Membrane traffic
SNARE After earliest reports in the 1980s (Novick et al. 1980; Balch et al. 1984), SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) have been identified as the key elements in membrane fusion. SNAREs are a family of proteins with 100–300 amino acids. They can be characterized by a roughly 60 residues length domain, called SNARE motif (Weimbs et al. 1997). The hetero-oligomeric interactions between SNARE motifs help to form a coiledcoil structure, which leads to the SNARE complex-forming during membrane fusion. According to their subcellular localization, SNAREs have been classified as t (target)- and v (vesicle)-SNAREs. Based on the conserved residues in the central layer of the SNARE complex, they can also be classified as Q (glutamine)- and R (arginine)- SNAREs (Fasshauer et al. 1998). Q-SNAREs can be further classified into four types, Qa-, Qb-, Qc-, and Qb + c-SNAREs. Most of the Q-SNAREs consist of an N terminal autoregulatory domain, a SNARE motif, and a C terminal transmembrane domain. QaSNAREs are initially described in synaptic exocytosis, so they are also named as syntaxins (Bennett et al. 1992). In the N terminal domain of Qa-SNAREs, there are three helices called the Ha, Hb, and Hc (or jointly Habc) domains, and * Ben Zhang [email protected] 1
School of Life Science, Shanxi University, Taiyuan 030006, Shanxi, China
these domains are folded into three helical bundles which mimic the parallel four-helix bundle of the SNARE complex (Rehman and Sansebastiano 2014). Qb- and Qc-SNAREs also contain an N terminal domain similar to that of QaSNARE (Hong 2005). The Qb + c-SNAREs contain both Qb- and Qc-SNARE motifs (Lipka et al. 2007), like the neuronal SNARE SNAP25. R-SNAREs are known as vesicle-associated membrane proteins (VAMPs). VAMPs also have three regions, including an N terminal domain, an R-SNARE motif, and a C terminal transmembrane domain. According to the length of N terminus, VAMPs can be subdivided into two groups: short VAMPs (brevins) and long VAMPs (longins) (Rossi et al. 2004). The longin domain forms a closed globular conformation and regulates the subcellular location of VAMPs by binding w
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