CDP1, a novel component of chloroplast division site positioning system in Arabidopsis

Zhang, Min; Hu, Yong; Jia, Jingjing; Li, Dapeng; Zhang, Runjie; Gao, Hongbo

doi:10.1038/cr.2009.78

Cited by 41 publications

(53 citation statements)

References 57 publications

(92 reference statements)

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“…Interestingly, the localization of FtsZ in PARC6 overexpression lines (Fig. 5) resembled that of a PARC6-GFP fusion protein overexpressed in wild-type plants (Zhang et al, 2009), consistent with our data showing PARC6-FtsZ2 colocalization in S. pombe (Figs. 3E and 4).…”

Section: Discussionsupporting

confidence: 80%

“…Consistent with these phenotypes, overexpression of both PARC6 and ARC3 in vivo had a similar inhibitory effect on FtsZ assembly and chloroplast division ( Fig. 5; Zhang et al, 2009). However, PARC6 did not inhibit FtsZ2 assembly in S. pombe (Figs.…”

Section: Discussionsupporting

confidence: 63%

“…This downstream factor was subsequently shown to be the nucleus-encoded chloroplast division protein PARALOG OF ARC6 (PARC6; Glynn et al, 2009), also called CDP1 (Zhang et al, 2009) and ARC6H (Ottesen et al, 2010). parc6 mutants exhibited mislocalization of PDV1 but not PDV2, demonstrating a specific role for PARC6 in PDV1 positioning.…”

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confidence: 99%

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Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division Complex and Negative Regulation of FtsZ Assembly

et al. 2015

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Chloroplast division is driven by the simultaneous constriction of the inner FtsZ ring (Z ring) and the outer DRP5B ring. The assembly and constriction of these rings in Arabidopsis (Arabidopsis thaliana) are coordinated partly through the inner envelope membrane protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS6 (ARC6). Previously, we showed that PARC6 (PARALOG OF ARC6), also in the inner envelope membrane, negatively regulates FtsZ assembly and acts downstream of ARC6 to position the outer envelope membrane protein PLASTID DIVISION1 (PDV1), which functions together with its paralog PDV2 to recruit DYNAMIN-RELATED PROTEIN 5B (DRP5B) from a cytosolic pool to the outer envelope membrane. However, whether PARC6, like ARC6, also functions in coordination of the chloroplast division contractile complexes was unknown. Here, we report a detailed topological analysis of Arabidopsis PARC6, which shows that PARC6 has a single transmembrane domain and a topology resembling that of ARC6. The newly identified stromal region of PARC6 interacts not only with ARC3, a direct inhibitor of Z-ring assembly, but also with the Z-ring protein FtsZ2. Overexpression of PARC6 inhibits FtsZ assembly in Arabidopsis but not in a heterologous yeast system (Schizosaccharomyces pombe), suggesting that the negative regulation of FtsZ assembly by PARC6 is a consequence of its interaction with ARC3. A conserved carboxyl-terminal peptide in FtsZ2 mediates FtsZ2 interaction with both PARC6 and ARC6. Consistent with its role in the positioning of PDV1, the intermembrane space regions of PARC6 and PDV1 interact. These findings provide new insights into the functions of PARC6 and suggest that PARC6 coordinates the inner Z ring and outer DRP5B ring through interaction with FtsZ2 and PDV1 during chloroplast division.

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Section: Discussionsupporting

confidence: 80%

Section: Discussionsupporting

confidence: 63%

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Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division Complex and Negative Regulation of FtsZ Assembly

et al. 2015

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“…Impaired division is observed in plants overexpressing FTSZ1 by <3-fold (Stokes et al, 2000;Schmitz et al, 2009). Overexpression of several other plastid division proteins also causes related but distinct abnormalities in chloroplast division, FTSZ filament organization, and chloroplast morphology (Vitha et al, 2003;Maple et al, 2007;Zhang et al, 2009Zhang et al, , 2013. By contrast, overexpression of PDV1 and/or PDV2 has the opposite effect in that it results in an increased plastid division rate and smaller and more numerous plastids per cell (Okazaki et al, 2009).…”

Section: Plastid Division Defects In Escrt and Autophagy Mutantsmentioning

confidence: 99%

The Endosomal Protein CHARGED MULTIVESICULAR BODY PROTEIN1 Regulates the Autophagic Turnover of Plastids in Arabidopsis

et al. 2015

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Endosomal Sorting Complex Required for Transport (ESCRT)-III proteins mediate membrane remodeling and the release of endosomal intraluminal vesicles into multivesicular bodies. Here, we show that the ESCRT-III subunit paralogs CHARGED MULTIVESICULAR BODY PROTEIN1 (CHMP1A) and CHMP1B are required for autophagic degradation of plastid proteins in Arabidopsis thaliana. Similar to autophagy mutants, chmp1a chmp1b (chmp1) plants hyperaccumulated plastid components, including proteins involved in plastid division. The autophagy machinery directed the release of bodies containing plastid material into the cytoplasm, whereas CHMP1A and B were required for delivery of these bodies to the vacuole. Autophagy was upregulated in chmp1 as indicated by an increase in vacuolar green fluorescent protein (GFP) cleavage from the autophagic reporter GFP-ATG8. However, autophagic degradation of the stromal cargo RECA-GFP was drastically reduced in the chmp1 plants upon starvation, suggesting that CHMP1 mediates the efficient delivery of autophagic plastid cargo to the vacuole. Consistent with the compromised degradation of plastid proteins, chmp1 plastids show severe morphological defects and aberrant division. We propose that CHMP1 plays a direct role in the autophagic turnover of plastid constituents.

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“…1). Apart from ARC3 and MCD1 the Chloroplast Division site Positioning 1 (AtCDP1) protein in Arabidopsis has also been shown to be associated with Z-ring placement (Zhang et al 2009). In line with previous Wndings, AtCDP1 interacts with ARC3 suggesting the presence of a Min/ARC3/AtCDP1 protein complex mediating correct Z-ring placement.…”

Section: Protein Complex Assembly and Regulationmentioning

confidence: 99%

Emerging facets of plastid division regulation

Basak

Møller

2012

Planta

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Plastids are complex organelles that are integrated into the plant host cell where they diVerentiate and divide in tune with plant diVerentiation and development. In line with their prokaryotic origin, plastid division involves both evolutionary conserved proteins and proteins of eukaryotic origin where the host has acquired control over the process. The plastid division apparatus is spatially separated between the stromal and the cytosolic space but where clear coordination mechanisms exist between the two machineries. Our knowledge of the plastid division process has increased dramatically during the past decade and recent Wndings have not only shed light on plastid division enzymology and the formation of plastid division complexes but also on the integration of the division process into a multicellular context. This review summarises our current knowledge of plastid division with an emphasis on biochemical features, the functional assembly of protein complexes and regulatory features of the overall process.

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CDP1, a novel component of chloroplast division site positioning system in Arabidopsis

Cited by 41 publications

References 57 publications

Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division Complex and Negative Regulation of FtsZ Assembly

Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division Complex and Negative Regulation of FtsZ Assembly

The Endosomal Protein CHARGED MULTIVESICULAR BODY PROTEIN1 Regulates the Autophagic Turnover of Plastids in Arabidopsis

Emerging facets of plastid division regulation

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