title: The OsSec18 complex interacts with P0(P1-P2)2 to regulate vacuolar morphology in rice endosperm cell.
abstract: BACKGROUND
  Sec18p/N-ethylmaleimide-sensitive factor (NSF) is a conserved eukaryotic ATPase, which primarily functions in vesicle membrane fusion from yeast to human. However, the function of the OsSec18 gene, a homologue of NSF in rice, remains unknown.
  
  
  RESULTS
  In the present study, we investigated the function of OsSec18 in rice and found that OsSec18 complements the temperature-sensitive phenotype and interferes with vacuolar morphogenesis in yeast. Overexpression of OsSec18 in rice decreased the plant height and 1000-grain weight and altered the morphology of the protein bodies. Further examination revealed that OsSec18 presented as a 290-kDa complex in rice endosperm cells. Moreover, Os60sP0 was identified a component of this complex, demonstrating that the OsSec18 complex contains another complex of P0(P1-P2)2 in rice endosperm cells. Furthermore, we determined that the N-terminus of OsSec18 can interact with the N- and C-termini of Os60sP0, whereas the C-terminus of OsSec18 can only interact with the C-terminus of Os60sP0.
  
  
  CONCLUSIONS
  Our results revealed that the OsSec18 regulates vacuolar morphology in both yeast and rice endosperm cell and the OsSec18 interacts with P0(P1-P2)2 complex in rice endosperm cell.
authors.forename: Yunfang
authors.initials: Y
authors.lastname: Sun
authors.forename: Tingting
authors.initials: T
authors.lastname: Ning
authors.forename: Zhenwei
authors.initials: Z
authors.lastname: Liu
authors.forename: Jianlei
authors.initials: J
authors.lastname: Pang
authors.forename: Daiming
authors.initials: D
authors.lastname: Jiang
authors.forename: Zhibin
authors.initials: Z
authors.lastname: Guo
authors.forename: Gaoyuan
authors.initials: G
authors.lastname: Song
authors.forename: Daichang
authors.initials: D
authors.lastname: Yang
mesh_terms: D000251:Adenosine Triphosphatases; D056625:Endosperm / Q000166:cytology* / Q000378:metabolism* / Q000648:ultrastructure; D020869:Gene Expression Profiling; D018506:Gene Expression Regulation, Plant; D005816:Genetic Complementation Test; D008561:Membrane Fusion; D008970:Molecular Weight; D046912:Multiprotein Complexes / Q000378:metabolism*; D009154:Mutation / Q000235:genetics; D009928:Organ Specificity / Q000235:genetics; D012275:Oryza / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D010641:Phenotype; D010940:Plant Proteins / Q000378:metabolism*; D030821:Plants, Genetically Modified; D011485:Protein Binding; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014617:Vacuoles / Q000378:metabolism* / Q000648:ultrastructure; D033921:Vesicular Transport Proteins
chemical_list: D046912:Multiprotein Complexes; D010940:Plant Proteins; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins; D000251:Adenosine Triphosphatases; C064404:SEC18 protein, S cerevisiae
references.citation: J Biol Chem. 1999 Apr 16;274(16):10677-80
references.pmid: 10196135
references.citation: J Biol Chem. 2001 Nov 30;276(48):45145-52
references.pmid: 11577089
references.citation: Nat Genet. 2005 May;37(5):501-6
references.pmid: 15806101
references.citation: Plant Cell Physiol. 2006 Sep;47(9):1187-94
references.pmid: 16926167
references.citation: FEBS Lett. 2007 May 22;581(11):2140-9
references.pmid: 17397838
references.citation: Cell. 2007 Sep 21;130(6):1057-70
references.pmid: 17889650
references.citation: Oncogene. 2008 Jan 10;27(3):332-8
references.pmid: 17621266
references.citation: Methods Mol Biol. 2009;479:235-45
references.pmid: 19083184
references.citation: Plant Cell. 2012 Dec;24(12):5058-73
references.pmid: 23263768
references.citation: J Biol Chem. 2013 Aug 9;288(32):23436-45
references.pmid: 23775070
references.citation: Int Rev Cytol. 1991;124:103-36
references.pmid: 2001915
references.citation: Biochimie. 1991 Jul-Aug;73(7-8):861-70
references.pmid: 1742361
references.citation: J Cell Biol. 1992 May;117(3):531-8
references.pmid: 1315316
references.citation: Cancer Res. 1992 Jun 1;52(11):3067-72
references.pmid: 1350508
references.citation: Cell. 1993 Nov 5;75(3):409-18
references.pmid: 8221884
references.citation: J Biol Chem. 1994 Jun 3;269(22):15689-96
references.pmid: 8195220
references.citation: Plant Physiol. 1994 Jun;105(2):753-4
references.pmid: 8066137
references.citation: Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5630-4
references.pmid: 7777561
references.citation: Yeast. 1995 Apr 15;11(4):355-60
references.pmid: 7785336
references.citation: Plant Physiol. 1998 Jun;117(2):407-15
references.pmid: 9625693
references.citation: Neuron. 1998 Jul;21(1):87-97
references.pmid: 9697854
references.citation: Neuron. 1998 Jul;21(1):99-110
references.pmid: 9697855
references.citation: Nucleic Acids Res. 2002 Jun 15;30(12):2620-7
references.pmid: 12060678
references.citation: Planta. 2003 Feb;216(4):597-603
references.pmid: 12569401
references.citation: Mol Biol Cell. 2000 Jul;11(7):2251-65
references.pmid: 10888666
references.citation: Cancer Res. 1999 Oct 1;59(19):4990-6
references.pmid: 10519413