Activation of the Rab7 GTPase by the MON1-CCZ1 Complex Is Essential for PVC-to-Vacuole Trafficking and Plant Growth in Arabidopsis . Issue 5 (13th May 2014)
- Record Type:
- Journal Article
- Title:
- Activation of the Rab7 GTPase by the MON1-CCZ1 Complex Is Essential for PVC-to-Vacuole Trafficking and Plant Growth in Arabidopsis . Issue 5 (13th May 2014)
- Main Title:
- Activation of the Rab7 GTPase by the MON1-CCZ1 Complex Is Essential for PVC-to-Vacuole Trafficking and Plant Growth in Arabidopsis
- Authors:
- Cui, Yong
Zhao, Qiong
Gao, Caiji
Ding, Yu
Zeng, Yonglun
Ueda, Takashi
Nakano, Akihiko
Jiang, Liwen - Abstract:
- Abstract : This work identifies the Arabidopsis MON1 and CCZ1 proteins as forming a dimeric complex that functions as a Rab5 effector and a Rab7 GEF to mediate Rab5-to-Rab7 conversion on PVCs. Arabidopsis Rab7 and mon1 mutants contained enlarged PVCs and fragmented vacuoles, and exhibited defects in vacuolar trafficking and retarded-growth phenotypes. Abstract: Rab GTPases serve as multifaceted organizers during vesicle trafficking. Rab7, a member of the Rab GTPase family, has been shown to perform various essential functions in endosome trafficking and in endosome-to-lysosome trafficking in mammalian systems. The Arabidopsis thaliana genome encodes eight putative Rab7 homologs; however, the detailed function and activation mechanism of Rab7 in plants remain unknown. Here, we demonstrate that Arabidopsis RABG3f, a member of the plant Rab7 small GTPase family, localizes to prevacuolar compartments (PVCs) and the tonoplast. The proper activation of Rab7 is essential for both PVC-to-vacuole trafficking and vacuole biogenesis. Expression of a dominant-negative Rab7 mutant (RABG3f T22N ) induces the formation of enlarged PVCs and affects vacuole morphology in plant cells. We also identify Arabidopsis MON1 (MONENSIN SENSITIVITY1) and CCZ1 (CALCIUM CAFFEINE ZINC SENSITIVITY1) proteins as a dimeric complex that functions as the Rab7 guanine nucleotide exchange factor. The MON1-CCZ1 complex also serves as the Rab5 effector to mediate Rab5-to-Rab7 conversion on PVCs. Loss ofAbstract : This work identifies the Arabidopsis MON1 and CCZ1 proteins as forming a dimeric complex that functions as a Rab5 effector and a Rab7 GEF to mediate Rab5-to-Rab7 conversion on PVCs. Arabidopsis Rab7 and mon1 mutants contained enlarged PVCs and fragmented vacuoles, and exhibited defects in vacuolar trafficking and retarded-growth phenotypes. Abstract: Rab GTPases serve as multifaceted organizers during vesicle trafficking. Rab7, a member of the Rab GTPase family, has been shown to perform various essential functions in endosome trafficking and in endosome-to-lysosome trafficking in mammalian systems. The Arabidopsis thaliana genome encodes eight putative Rab7 homologs; however, the detailed function and activation mechanism of Rab7 in plants remain unknown. Here, we demonstrate that Arabidopsis RABG3f, a member of the plant Rab7 small GTPase family, localizes to prevacuolar compartments (PVCs) and the tonoplast. The proper activation of Rab7 is essential for both PVC-to-vacuole trafficking and vacuole biogenesis. Expression of a dominant-negative Rab7 mutant (RABG3f T22N ) induces the formation of enlarged PVCs and affects vacuole morphology in plant cells. We also identify Arabidopsis MON1 (MONENSIN SENSITIVITY1) and CCZ1 (CALCIUM CAFFEINE ZINC SENSITIVITY1) proteins as a dimeric complex that functions as the Rab7 guanine nucleotide exchange factor. The MON1-CCZ1 complex also serves as the Rab5 effector to mediate Rab5-to-Rab7 conversion on PVCs. Loss of functional MON1 causes the formation of enlarged Rab5-positive PVCs that are separated from Rab7-positive endosomes. Similar to the dominant-negative Rab7 mutant, the mon1 mutants show pleiotropic growth defects, fragmented vacuoles, and altered vacuolar trafficking. Thus, Rab7 activation by the MON1-CCZ1 complex is critical for vacuolar trafficking, vacuole biogenesis, and plant growth. … (more)
- Is Part Of:
- The Plant Cell. Volume 26:Issue 5(2014)
- Journal:
- The Plant Cell
- Issue:
- Volume 26:Issue 5(2014)
- Issue Display:
- Volume 26, Issue 5 (2014)
- Year:
- 2014
- Volume:
- 26
- Issue:
- 5
- Issue Sort Value:
- 2014-0026-0005-0000
- Page Start:
- 2080
- Page End:
- 2097
- Publication Date:
- 2014-05-13
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.114.123141 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16361.xml