New Gateway-compatible vectors for a high-throughput protein–protein interaction analysis by a bimolecular fluorescence complementation (BiFC) assay in plants and their application to a plant clathrin structure analysis

References

• Ghosh I, Hamilton AD, Regan L. Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein. J. Am. Chem. Soc. 2000;122:5658–5659.10.1021/ja994421w
   Web of Science ®Google Scholar
• Xu Y, Piston DW, Johnson CH. A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proc. Natl. Acad. Sci. USA. 1999;96:151–156.
   Google Scholar
• Heim R, Tsien RY. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 1996;6:178–182.10.1016/S0960-9822(02)00450-5
   PubMed Web of Science ®Google Scholar
• Kodama Y, Hu CD. Bimolecular fluorescence complementation (BiFC): a 5-year update and future perspectives. BioTechniques. 2012;53:285–298.
   PubMed Web of Science ®Google Scholar
• Shyu YJ, Liu H, Deng X, et al. Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions. BioTechniques. 2006;40:61–66.10.2144/000112036
   PubMed Web of Science ®Google Scholar
• Kerppola TK. Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu. Rev. Biophys. 2008;37:465–487.10.1146/annurev.biophys.37.032807.125842
   PubMed Web of Science ®Google Scholar
• Shyu YJ, Hu CD. Fluorescence complementation: an emerging tool for biological research. Trends Biotechnol. 2008;26:622–630.10.1016/j.tibtech.2008.07.006
   PubMed Web of Science ®Google Scholar
• Hino T, Tanaka Y, Kawamukai M, et al. Two Sec13p homologs, AtSec13A and AtSec13B, redundantly contribute to the formation of COPII transport vesicles in Arabidopsis thaliana. Biosci. Biotechnol. Biochem. 2011;75:1848–1852.10.1271/bbb.110331
   PubMed Web of Science ®Google Scholar
• Ohashi K, Kiuchi T, Shoji K, et al. Visualization of cofilin-actin and Ras-Raf interactions by bimolecular fluorescence complementation assays using a new pair of split Venus fragments. BioTechniques. 2012;52:45–50.
   PubMed Web of Science ®Google Scholar
• Gookin TE, Assmann SM. Significant reduction of BiFC non-specific assembly facilitates in planta assessment of heterotrimeric G-protein interactors. Plant J. 2014;80:553–567.10.1111/tpj.2014.80.issue-3
   PubMed Web of Science ®Google Scholar
• Zacharias DA, Violin JD, Newton AC, et al. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 2002;296:913–916.10.1126/science.1068539
   PubMed Web of Science ®Google Scholar
• Nakagawa T, Kurose T, Hino T, et al. Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation. J. Biosci. Bioeng. 2007;104:34–41.10.1263/jbb.104.34
   PubMed Web of Science ®Google Scholar
• Bonifacino JS, Traub LM. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 2003;72:395–447.10.1146/annurev.biochem.72.121801.161800
   PubMed Web of Science ®Google Scholar
• Torii T, Miyamoto Y, Sanbe A, et al. Cytohesin-2/ARNO, through its interaction with focal adhesion adaptor protein paxillin, regulates preadipocyte migration via the downstream activation of Arf6. J. Biol. Chem. 2010;285:24270–24281.10.1074/jbc.M110.125658
   PubMed Web of Science ®Google Scholar
• Standley DM, Toh H, Nakamura H. ASH structure alignment package: sensitivity and selectivity in domain classification. BMC Bioinf. 2007;8:116.10.1186/1471-2105-8-116
   PubMed Web of Science ®Google Scholar
• Fujimoto M, Ueda T. Conserved and plant-unique mechanisms regulating plant post-Golgi traffic. Front. Plant Sci. 2012;3:197.
   PubMed Web of Science ®Google Scholar
• Kirchhausen T, Owen D, Harrison SC. Molecular structure, function, and dynamics of clathrin-mediated membrane traffic. Cold Spring Harb. Perspect. Biol. 2014;6:a016725.10.1101/cshperspect.a016725
   PubMed Web of Science ®Google Scholar
• Scheele U, Holstein SE. Functional evidence for the identification of an Arabidopsis clathrin light chain polypeptide. FEBS Lett. 2002;514:355–360.10.1016/S0014-5793(02)02439-0
   PubMed Web of Science ®Google Scholar
• Van Damme D, Gadeyne A, Vanstraelen M, et al. Adaptin-like protein TPLATE and clathrin recruitment during plant somatic cytokinesis occurs via two distinct pathways. Proc. Natl. Acad. Sci. USA. 2011;108:615–620.10.1073/pnas.1017890108
   PubMed Web of Science ®Google Scholar
• Chen CY, Reese ML, Hwang PK, et al. Clathrin light and heavy chain interface: α-helix binding superhelix loops via critical tryptophans. EMBO J. 2002;21:6072–6082.10.1093/emboj/cdf594
   PubMed Web of Science ®Google Scholar
• Hu CD, Chinenov Y, Kerppola TK. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell. 2002;9:789–798.10.1016/S1097-2765(02)00496-3
   PubMed Web of Science ®Google Scholar
• Ybe JA, Brodsky FM, Hofmann K, et al. Clathrin self-assembly is mediated by a tandemly repeated superhelix. Nature. 1999;399:371–375.10.1038/20708
   PubMed Web of Science ®Google Scholar
• Zeng MH, Liu SH, Yang MX, et al. Characterization of a gene encoding clathrin heavy chain in maize up-regulated by salicylic acid, abscisic acid and high boron supply. Int. J. Mol. Sci. 2013;14:15179–15198.10.3390/ijms140715179
   PubMed Web of Science ®Google Scholar
• Baisa GA, Mayers JR, Bednarek SY. Budding and braking news about clathrin-mediated endocytosis. Curr. Opin. Plant Biol. 2013;16:718–725.10.1016/j.pbi.2013.09.005
   PubMed Web of Science ®Google Scholar
• Ybe JA, Greene B, Liu SH, et al. Clathrin self-assembly is regulated by three light-chain residues controlling the formation of critical salt bridges. EMBO J. 1998;17:1297–1303.10.1093/emboj/17.5.1297
   PubMed Web of Science ®Google Scholar
• Kirchhausen T, Toyoda T. Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers. J. Biol. Chem. 1993;268:10268–10273.
   PubMed Web of Science ®Google Scholar
• Fotin A, Cheng Y, Sliz P, et al. Molecular model for a complete clathrin lattice from electron cryomicroscopy. Nature. 2004;432:573–579.10.1038/nature03079
   PubMed Web of Science ®Google Scholar