VARICOSE, a WD-domain protein, is required for leaf blade development

Deyholos, Michael K.; Cavaness, G. Frank; Hall, B. Vincent; King, E. C.; Punwani, Jayson A.; Norman, Jaimie Van; Sieburth, Leslie

doi:10.1242/dev.00909

Cited by 50 publications

(54 citation statements)

References 51 publications

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“…The phenotypic similarities between hve/hve and axr1-12/axr1-12 plants, including their bushy inflorescence and low fertility, point to a functional relationship between HVE and AXR1. We did not find significant differences in vascular density and number of branching points per surface unit between axr1-12/axr1-12 and hve-3/hve-3 first leaves [ Table 2; this aspect of the axr1 phenotype has been reported by Deyholos et al (Deyholos et al, 2003)]. However, the leaf epinasty of axr1-12 mutants (see Fig.…”

Section: Genetic Interactionssupporting

confidence: 54%

TheHVE/CAND1gene is required for the early patterning of leaf venation inArabidopsis

et al. 2006

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The hemivenata-1 (hve-1) recessive allele was isolated in a search for natural variations in the leaf venation pattern of Arabidopsis thaliana, where it was seen to cause extremely simple venation in vegetative leaves and cotyledons, increased shoot branching, and reduced root waving and fertility, traits that are reminiscent of some mutants deficient in auxin signaling. Reduced sensitivity to exogenous auxin was found in the hve-1 mutant, which otherwise displayed a wild-type response to auxin transport inhibitors. The HVE gene was positionally cloned and found to encode a CAND1 protein. The hve-1 mutation caused mis-splicing of the transcripts of the HVE/CAND1 gene and a vein phenotype indistinguishable from that of hve-2 and hve-3, two putatively null T-DNA alleles. Inflorescence size and fertility were more affected by hve-2 and hve-3, suggesting that hve-1 is hypomorphic. The simple venation pattern of hve plants seems to arise from an early patterning defect. We found that HVE/CAND1 binds to CULLIN1, and that the venation patterns of axr1 and hve mutants are similar, which suggest that ubiquitin-mediated auxin signaling is required for venation patterning in laminar organs, the only exception being cauline leaves. Our analyses of double mutant and transgenic plants indicated that auxin transport and perception act independently to pattern leaf veins, and that the HVE/CAND1 gene acts upstream of ATHB-8 at least in higher order veins, in a pathway that involves AXR1, but not LOP1, PIN1, CVP1 or CVP2.

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Section: Genetic Interactionssupporting

confidence: 54%

TheHVE/CAND1gene is required for the early patterning of leaf venation inArabidopsis

et al. 2006

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“…RNA extraction and cDNA template preparation were performed as described previously (Deyholos et al, 2003). For real-time RT-PCR, we used the Roche LightCycler and Roche FastStart DNA Master SYBR Green 1 master mix.…”

Section: Real-time Rt-pcr Analysismentioning

confidence: 99%

“…GUS staining reactions and auxin induction of DR5 expression were performed as described by Deyholos et al (2003), except that auxin treatment lasted 5 h (instead of 8), and control incubations were performed in liquid GM. The GUS staining reactions were terminated after 3 to 4 h, and tissue was fixed and cleared as described above.…”

Section: Gus Stainingmentioning

confidence: 99%

SCARFACEEncodes an ARF-GAP That Is Required for Normal Auxin Efflux and Vein Patterning inArabidopsis

et al. 2006

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To identify molecular mechanisms controlling vein patterns, we analyzed scarface (sfc) mutants. sfc cotyledon and leaf veins are largely fragmented, unlike the interconnected networks in wild-type plants. SFC encodes an ADP ribosylation factor GTPase activating protein (ARF-GAP), a class with well-established roles in vesicle trafficking regulation. Quadruple mutants of SCF and three homologs (ARF-GAP DOMAIN1, 2, and 4) showed a modestly enhanced vascular phenotype. Genetic interactions between sfc and pinoid and between sfc and gnom suggest a possible function for SFC in trafficking of auxin efflux regulators. Genetic analyses also revealed interaction with cotyledon vascular pattern2, suggesting that lipidbased signals may underlie some SFC ARF-GAP functions. To assess possible roles for SFC in auxin transport, we analyzed sfc roots, which showed exaggerated responses to exogenous auxin and higher auxin transport capacity. To determine whether PIN1 intracellular trafficking was affected, we analyzed PIN1:green fluorescent protein (GFP) dynamics using confocal microscopy in sfc roots. We found normal PIN1:GFP localization at the apical membrane of root cells, but treatment with brefeldin A resulted in PIN1 accumulating in smaller and more numerous compartments than in the wild type. These data suggest that SFC is required for normal intracellular transport of PIN1 from the plasma membrane to the endosome.

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“…The N-terminal and C-terminal globular domains are separated by a low-complexity region rich in serines (Ser-rich linker), which is thought to provide a flexible linker (Deyholos et al 2003;Fenger-Grøn et al 2005;Yu et al 2005;Xu et al 2006, Eulalio et al 2007c). In Homo.…”

Section: Introductionmentioning

confidence: 99%

The C-terminal region of Ge-1 presents conserved structural features required for P-body localization

Jinek

Eulálio²,

Lingel³

et al. 2008

RNA

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The removal of the 59 cap structure by the DCP1-DCP2 decapping complex irreversibly commits eukaryotic mRNAs to degradation. In human cells, the interaction between DCP1 and DCP2 is bridged by the Ge-1 protein. Ge-1 contains an Nterminal WD40-repeat domain connected by a low-complexity region to a conserved C-terminal domain. It was reported that the C-terminal domain interacts with DCP2 and mediates Ge-1 oligomerization and P-body localization. To understand the molecular basis for these functions, we determined the three-dimensional crystal structure of the most conserved region of the Drosophila melanogaster Ge-1 C-terminal domain. The region adopts an all a-helical fold related to ARM-and HEAT-repeat proteins. Using structure-based mutants we identified an invariant surface residue affecting P-body localization. The conservation of critical surface and structural residues suggests that the C-terminal region adopts a similar fold with conserved functions in all members of the Ge-1 protein family.

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VARICOSE, a WD-domain protein, is required for leaf blade development

Cited by 50 publications

References 51 publications

TheHVE/CAND1gene is required for the early patterning of leaf venation inArabidopsis

TheHVE/CAND1gene is required for the early patterning of leaf venation inArabidopsis

SCARFACEEncodes an ARF-GAP That Is Required for Normal Auxin Efflux and Vein Patterning inArabidopsis

The C-terminal region of Ge-1 presents conserved structural features required for P-body localization

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