Soybean mosaic virus (SMV), a member of the Potyvirus genus, is one of the most prevalent and devastating viral pathogens in soybean-growing regions worldwide. It is generally accepted that symptom development of a viral plant disease results from molecular interactions between the virus and its host plant. P3N-PIPO, as a trans-frame protein consisting of the amino-terminal half of P3 fused to PIPO of the Potyvirus, plays a key role of viral cell-to-cell movement. This study provides evidence that Golgi SNARE 12 (designated as GOS12) protein of soybean interacts with SMV P3N-PIPO via a two-hybrid yeast system by screening a soybean cDNA library. Bimolecular fluorescence complementation (BiFC) assay further confirmed the interaction, which occurred in the cytomembrane of Nicotiana benthamiana cells. We also confirmed that the domain involved in the interaction is PIPO domain of P3N-PIPO by two-hybrid yeast system and BiFC. It is possible that the GOS12 is an essential host factor for PD targeting of P3N-PIPO protein of potyvirus.
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http://dx.doi.org/10.1016/j.bbrc.2016.08.103 | DOI Listing |
Methods Mol Biol
January 2025
Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Functionally derivatized analogs of prenyl lipids are valuable tools for the detection and analysis of prenylated proteins. Using a biotinylated analog of geranylgeranyl, we previously identified Ykt6 as a substrate for a novel protein prenyltransferase, termed geranylgeranyltransferase type III (GGTase-III). Ykt6 is an evolutionarily highly conserved SNARE protein that regulates multiple intracellular trafficking pathways, including intra-Golgi trafficking and autophagosome-lysosome fusion.
View Article and Find Full Text PDFJ Cell Sci
January 2025
Department of Ophthalmology and Visual Sciences, University of New Mexico, Albuquerque, New Mexico 87131, Mexico.
The Rab11-Rabin8-Rab8 ciliogenesis complex regulates the expansion of cilia-derived light-sensing organelles, the rod outer segments, via post-Golgi rhodopsin transport carriers (RTCs). Rabin8, an effector of Rab11 and a nucleotide exchange factor (GEF) for Rab8, is phosphorylated at S272 by NDR2 kinase (aka STK38L), a canine erd gene product linked to the human ciliopathy Leber congenital amaurosis (LCA). Here, we define the step at which NDR2 phosphorylated Rabin8 regulates Rab11-Rab8 succession in X.
View Article and Find Full Text PDFFront Cell Dev Biol
December 2024
Program of Life and Environmental Science, Graduate School of Integral Science for Life, Hiroshima University, Hiroshima, Japan.
Polarized transport is essential for the construction of multiple plasma membrane domains within cells. photoreceptors serve as excellent model systems for studying the mechanisms of polarized transport. We conducted a comprehensive soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) screening of the fly genome using RNAi knockdown and CRISPR/Cas9 somatic knockout combined with the CoinFLP system to identify SNAREs involved in post-Golgi trafficking.
View Article and Find Full Text PDFNat Commun
November 2024
Division of Neurosciences and Cellular Structure, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
ARL5 is a member of the ARF family of small GTPases that is recruited to the trans-Golgi network (TGN) by another ARF-family member, ARFRP1, in complex with the transmembrane protein SYS1. ARL5 recruits its effector, the multisubunit tethering complex GARP, to promote SNARE-dependent fusion of endosome-derived retrograde transport carriers with the TGN. To further investigate the function of ARL5, we sought to identify additional effectors.
View Article and Find Full Text PDFbioRxiv
November 2024
University of Arkansas for Medical Sciences, Department of Physiology and Cell Biology, Little Rock, Arkansas, US.
Intracellular trafficking relies on small vesicular intermediates, though their specific role in Golgi function is still debated. To clarify this, we induced acute dysfunction of the Conserved Oligomeric Golgi (COG) complex and analyzed vesicles from cis, medial, and trans-Golgi compartments. Proteomic analysis of Golgi-derived vesicles from wild-type cells revealed distinct molecular profiles, indicating a robust recycling system for Golgi proteins.
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