Subcellular Dynamics and Role of <i>Arabidopsis</i> β-1,3-Glucanases in Cell-to-Cell Movement of Tobamoviruses

Zavaliev, Raul; Levy, Amit; Gera, A.; Epel, Bernard L.

doi:10.1094/mpmi-03-13-0062-r

Cited by 121 publications

(92 citation statements)

References 91 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Historically, BGs were mainly studied with respect to their role as pathogenesis-related (PR) proteins in the context of stress responses (Leubner-Metzger and Meins, 1999). For example, the Arabidopsis BG AtBG_ppap localizes to PD, affects callose accumulation at PD upon wounding and regulates PD flux (Levy et al, 2007;Zavaliev et al, 2013). More recently, however, it became clear that the two PD-localized BGs PdBG1 and PdBG2 play a prominent role in early lateral root formation through the regulation of PD conductivity by modulating callose accumulation at PD (Benitez-Alfonso et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

The cell wall-localized atypical β-1,3 glucanase ZERZAUST controls tissue morphogenesis in Arabidopsis thaliana

et al. 2017

View full text Add to dashboard Cite

Orchestration of cellular behavior in plant organogenesis requires integration of intercellular communication and cell wall dynamics. The underlying signaling mechanisms are poorly understood. Tissue morphogenesis in Arabidopsis depends on the receptor-like kinase STRUBBELIG. Mutations in ZERZAUST were previously shown to result in a strubbelig-like mutant phenotype. Here, we report on the molecular identification and functional characterization of ZERZAUST. We show that ZERZAUST encodes a putative GPIanchored β-1,3 glucanase suggested to degrade the cell wall polymer callose. However, a combination of in vitro, cell biological and genetic experiments indicate that ZERZAUST is not involved in the regulation of callose accumulation. Nonetheless, Fourier-transformed infraredspectroscopy revealed that zerzaust mutants show defects in cell wall composition. Furthermore, the results indicate that ZERZAUST represents a mobile apoplastic protein, and that its carbohydrate-binding module family 43 domain is required for proper subcellular localization and function whereas its GPI anchor is dispensable. Our collective data reveal that the atypical β-1,3 glucanase ZERZAUST acts in a non-cell-autonomous manner and is required for cell wall organization during tissue morphogenesis.

show abstract

Section: Discussionmentioning

confidence: 99%

The cell wall-localized atypical β-1,3 glucanase ZERZAUST controls tissue morphogenesis in Arabidopsis thaliana

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Although the ERdesmotubule continuum may target VRCs and associated MP from these junctions into adjacent cells, the MP may target PD also by an endosomal pathway that delivers MP to the PM around PD. This pathway may allow MP to interact with the PD-localized and glycosylphosphatidylinositol (GPI)-anchored beta-glucanase AtBG_-pap, which is proposed to control callose levels in PD and to play a role in virus movement (Zavaliev et al, 2013). The association of PD with underlying viral factors at microtubule:ER junctions/ERanchoring sites is consistent with the often-observed formation of 'paired bodies' or 'caps', thus the accumulation of VRCs and viral proteins on both sides of PD behind the virus front (Kotlizky et al, 2001;Szécsi et al, 1999;Tilsner et al, 2013).…”

Section: The Targeting Of Plasmodesmata Involves Additional Membrane mentioning

confidence: 99%

Plant virus replication and movement

2015

View full text Add to dashboard Cite

Replication and intercellular spread of viruses depend on host mechanisms supporting the formation, transport and turnover of functional complexes between viral genomes, virus-encoded products and cellular factors. To enhance these processes, viruses assemble and replicate in membrane-associated complexes that may develop into "virus factories" or "viroplasms" in which viral components and host factors required for replication are concentrated. Many plant viruses replicate in association with the cortical ER-actin network that is continuous between cells through plasmodesmata. The replication complexes can be highly organized and supported by network interactions between the viral genome and the virus-encoded proteins. Intracellular PD targeting of replication complexes links the process of movement to replication and provides specificity for transport of the viral genome by the virus-encoded movement proteins. The formation and trafficking of replication complexes and also the development and anchorage of replication factories involves important roles of the cortical cytoskeleton and associated motor proteins.

show abstract

“…This implies that the activity of callose biosynthetic (callose synthases, CalS) and degrading enzymes (glycosyl hydrolase family 17, GHL17) must be rapidly and efficiently regulated at PD sites. Not surprisingly, PD-associated CalS and GHL17 proteins have been recently identified (Guseman et al, 2010; Vaten et al, 2011; Slewinski et al, 2012; Benitez-Alfonso et al, 2013; Zavaliev et al, 2013). …”

Section: Introductionmentioning

confidence: 99%

A phylogenetic approach to study the origin and evolution of plasmodesmata-localized glycosyl hydrolases family 17

Gaudioso-Pedraza

Benitez‐Alfonso

2014

Front. Plant Sci.

View full text Add to dashboard Cite

Colonization of the land by plants required major modifications in cellular structural composition and metabolism. Intercellular communication through plasmodesmata (PD) plays a critical role in the coordination of growth and cell activities. Changes in the form, regulation or function of these channels are likely linked to plant adaptation to the terrestrial environments. Constriction of PD aperture by deposition of callose is the best-studied mechanism in PD regulation. Glycosyl hydrolases family 17 (GHL17) are callose degrading enzymes. In Arabidopsis this is a large protein family, few of which have been PD-localized. The objective here is to identify correlations between evolution of this protein family and their role at PD and to use this information as a tool to predict the localization of candidates isolated in a proteomic screen. With this aim, we studied phylogenetic relationship between Arabidopsis GHL17 sequences and those isolated from fungi, green algae, mosses and monocot representatives. Three distinct phylogenetic clades were identified. Clade alpha contained only embryophytes sequences suggesting that this subgroup appeared during land colonization in organisms with functional PD. Accordingly, all PD-associated GHL17 proteins identified so far in Arabidopsis thaliana and Populus are grouped in this ‘embryophytes only’ phylogenetic clade. Next, we tested the use of this knowledge to discriminate between candidates isolated in the PD proteome. Transient and stable expression of GFP protein fusions confirmed PD localization for candidates contained in clade alpha but not for candidates contained in clade beta. Our results suggest that GHL17 membrane proteins contained in the alpha clade evolved and expanded during land colonization to play new roles, among others, in PD regulation.

show abstract

Subcellular Dynamics and Role of Arabidopsis β-1,3-Glucanases in Cell-to-Cell Movement of Tobamoviruses

Cited by 121 publications

References 91 publications

The cell wall-localized atypical β-1,3 glucanase ZERZAUST controls tissue morphogenesis in Arabidopsis thaliana

The cell wall-localized atypical β-1,3 glucanase ZERZAUST controls tissue morphogenesis in Arabidopsis thaliana

Plant virus replication and movement

A phylogenetic approach to study the origin and evolution of plasmodesmata-localized glycosyl hydrolases family 17

Contact Info

Product

Resources

About