Rha1, an Arabidopsis Rab5 Homolog, Plays a Critical Role in the Vacuolar Trafficking of Soluble Cargo Proteins

Overview

Journal Plant Cell

Publisher Oxford University Press

Specialties Biology
Cell Biology

Date 2003 May 2

PMID 12724533

Citations 93

Authors

Eun Ju Sohn

Eol Sun Kim

Min Zhao

Soo Jin Kim

Hyeran Kim

Yong-Woo Kim

Yong Jik Lee

Stefan Hillmer

Uik Sohn

Liwen Jiang

Inhwan Hwang

Affiliations

Soon will be listed here.

Abstract

Rab proteins are members of the Ras superfamily of small GTP binding proteins and play important roles in various intracellular trafficking steps. We investigated the role of Rha1, an Arabidopsis Rab5 homolog, in intracellular trafficking in Arabidopsis protoplasts. In the presence of a dominant-negative mutant of Rha1, soluble vacuolar cargo proteins such as sporamin:green fluorescent protein (Spo:GFP) and Arabidopsis aleurain like protein:GFP are not delivered to the central vacuole; instead, they accumulate as a diffuse or punctate staining pattern within the cell. Spo:GFP at the punctate stains observed in the presence of hemagglutinin:Rha1[S24N] is colocalized with endogenous vacuolar sorting receptor (VSR(At-1)), which is known to localize primarily to the prevacuolar compartment, whereas Spo:GFP in the diffuse pattern is associated with tonoplasts. Furthermore, expression of Rha1[S24N] causes the secretion of a portion of the vacuolar proteins into medium. However, the inhibitory effect of Rha1[S24N] on vacuolar trafficking is relieved partially by coexpressed wild-type Rha1. Based on these results, we propose that Rha1 plays a critical role in the trafficking of soluble cargoes from the prevacuolar compartment to the central vacuole.

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References

Piper R, Luzio J . Late endosomes: sorting and partitioning in multivesicular bodies. Traffic. 2001; 2(9):612-21. DOI: 10.1034/j.1600-0854.2001.20904.x. View

Ueda T, Yamaguchi M, Uchimiya H, Nakano A . Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana. EMBO J. 2001; 20(17):4730-41. PMC: 125591. DOI: 10.1093/emboj/20.17.4730. View

Sheen J . Signal transduction in maize and Arabidopsis mesophyll protoplasts. Plant Physiol. 2001; 127(4):1466-75. PMC: 1540179. View

Park C, Shin R, Park J, Lee G, You J, Paek K . Induction of pepper cDNA encoding a lipid transfer protein during the resistance response to tobacco mosaic virus. Plant Mol Biol. 2002; 48(3):243-54. DOI: 10.1023/a:1013383329361. View

Li Y, Rogers S, Tse Y, Lo S, Sun S, Jauh G . BP-80 and homologs are concentrated on post-Golgi, probable lytic prevacuolar compartments. Plant Cell Physiol. 2002; 43(7):726-42. DOI: 10.1093/pcp/pcf085. View

Lee M, Min M, Lee Y, Jin J, Shin D, Kim D . ADP-ribosylation factor 1 of Arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulum morphology in Arabidopsis. Plant Physiol. 2002; 129(4):1507-20. PMC: 166739. DOI: 10.1104/pp.003624. View

Nakano A, Muramatsu M . A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J Cell Biol. 1989; 109(6 Pt 1):2677-91. PMC: 2115904. DOI: 10.1083/jcb.109.6.2677. View

Chavrier P, Parton R, Hauri H, Simons K, Zerial M . Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell. 1990; 62(2):317-29. DOI: 10.1016/0092-8674(90)90369-p. View

Morimoto B, Chuang C, Koshland Jr D . Molecular cloning of a member of a new class of low-molecular-weight GTP-binding proteins. Genes Dev. 1991; 5(12B):2386-91. DOI: 10.1101/gad.5.12b.2386. View

10.

Robinson M, Kreis T . Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators. Cell. 1992; 69(1):129-38. DOI: 10.1016/0092-8674(92)90124-u. View

11.

Bucci C, Parton R, Mather I, Stunnenberg H, Simons K, Hoflack B . The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell. 1992; 70(5):715-28. DOI: 10.1016/0092-8674(92)90306-w. View

12.

Tisdale E, Bourne J, Khosravi-Far R, Der C, Balch W . GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. J Cell Biol. 1992; 119(4):749-61. PMC: 2289685. DOI: 10.1083/jcb.119.4.749. View

13.

Yoshihisa T, Barlowe C, Schekman R . Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science. 1993; 259(5100):1466-8. DOI: 10.1126/science.8451644. View

14.

Anuntalabhochai S, Terryn N, Van Montagu M, Inze D . Molecular characterization of an Arabidopsis thaliana cDNA encoding a small GTP-binding protein, Rha1. Plant J. 1991; 1(2):167-74. View

15.

Waters M, Pfeffer S . Membrane tethering in intracellular transport. Curr Opin Cell Biol. 1999; 11(4):453-9. DOI: 10.1016/s0955-0674(99)80065-9. View

16.

Corvera S, DArrigo A, Stenmark H . Phosphoinositides in membrane traffic. Curr Opin Cell Biol. 1999; 11(4):460-5. DOI: 10.1016/S0955-0674(99)80066-0. View

17.

Pfeffer S . Rab GTPases: master regulators of membrane trafficking. Curr Opin Cell Biol. 1994; 6(4):522-6. DOI: 10.1016/0955-0674(94)90071-x. View

18.

Chen Y, Holcomb C, Moore H . Expression and localization of two low molecular weight GTP-binding proteins, Rab8 and Rab10, by epitope tag. Proc Natl Acad Sci U S A. 1993; 90(14):6508-12. PMC: 46961. DOI: 10.1073/pnas.90.14.6508. View

19.

Ullrich O, Stenmark H, Alexandrov K, Huber L, Kaibuchi K, Sasaki T . Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins. J Biol Chem. 1993; 268(24):18143-50. View

20.

Terryn N, Arias M, Engler G, Tire C, Villarroel R, Van Montagu M . rha1, a gene encoding a small GTP binding protein from Arabidopsis, is expressed primarily in developing guard cells. Plant Cell. 1993; 5(12):1761-9. PMC: 160402. DOI: 10.1105/tpc.5.12.1761. View