A membrane-anchored E-type endo-1,4-β-glucanase is localized on Golgi and plasma membranes of higher plants

Brummell, David A.; Catalá, Carmen; Lashbrook, Coralie C.; Bennett, A. B.

doi:10.1073/pnas.94.9.4794

Cited by 126 publications

(83 citation statements)

References 31 publications

(47 reference statements)

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“…In apparent contrast with the in situ immunolabeling results, immunoblotting revealed KOR1 in fractions enriched for plasma membrane markers obtained by sucrose density gradients (Brummell et al, 1997), free-flow electrophoresis (Nicol et al, 1998), or two-phase partitioning (S. Vernhettes, unpublished data). Because no endosomal markers were used in these experiments, it cannot be excluded that these plasma membraneenriched fractions contained membranes of endosomal origin.…”

Section: Discussion Kor1 Endo-14-b-d-glucanase Cycles Through Subcelcontrasting

confidence: 57%

“…In contrast with other endo-1,4-b-D-glucanases, KOR1 is an integral type II membrane protein. Sucrose density gradients on microsomes from tomato (Lycopersicon esculentum) seedlings and free-flow electrophoresis on membranes from Arabidopsis cell suspension cultures localized KOR1 at least partially to the plasma membrane but also to intracellular fractions (Brummell et al, 1997;Nicol et al, 1998). Zuo et al (2000) expressed a KOR1-green fluorescent protein (GFP) fusion protein in tobacco (Nicotiana tabacum) BY2 cells and observed the accumulation of the fusion protein in the nascent cell plate and in punctate intracellular structures.…”

Section: Introductionmentioning

confidence: 99%

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AnArabidopsisEndo-1,4-β-d-Glucanase Involved in Cellulose Synthesis Undergoes Regulated Intracellular Cycling[W]

et al. 2005

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The synthesis of cellulose microfibrils requires the presence of a membrane-bound endo-1,4-b-D-glucanase, KORRIGAN1 (KOR1). Although the exact biochemical role of KOR1 in cellulose synthesis is unknown, we used the protein as a marker to explore the potential involvement of subcellular transport processes in cellulose synthesis. Using immunofluorescence and a green fluorescent protein (GFP)-KOR1 fusion that complemented the phenotype conferred by the kor1-1 mutant, we investigated the distribution of KOR1 in epidermal cells in the root meristem. KOR1 was localized in intracellular compartments corresponding to a heterogeneous population of organelles, which comprised the Golgi apparatus, FM4-64-labeled compartments referred to as early endosomes, and, in the case of GFP-KOR1, the tonoplast. Inhibition of cellulose synthesis by isoxaben promoted a net redistribution of GFP-KOR1 toward a homogeneous population of compartments, distinct from early endosomes, which were concentrated close to the plasma membrane facing the root surface. A redistribution of GFP-KOR1 away from early endosomes was also observed in the same cells at later stages of cell elongation. A subpopulation of GFP-KOR1-containing compartments followed trajectories along the plasma membrane, and this motility required intact microtubules. These observations demonstrate that the deposition of cellulose, like chitin synthesis in yeast, involves the regulated intracellular cycling of at least one enzyme required for its synthesis.

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Section: Discussion Kor1 Endo-14-b-d-glucanase Cycles Through Subcelcontrasting

confidence: 57%

Section: Introductionmentioning

confidence: 99%

AnArabidopsisEndo-1,4-β-d-Glucanase Involved in Cellulose Synthesis Undergoes Regulated Intracellular Cycling[W]

et al. 2005

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“…The tomato (Solanum lycopersicum) GH9A1 homolog Sl-GH9A1 was localized to both the Golgi and the plasma membrane by Suc gradient fractionation of tomato root microsomal membranes (Brummell et al, 1997). Partially consistent with this observation, AtGH9A1-GFP (for green fluorescent protein) showed a punctate pattern in interphase cells and was observed at the cell plate during cytokinesis of tobacco (Nicotiana tabacum) BY2 cells (Zuo et al, 2000).…”

Section: Introductionsupporting

confidence: 62%

Thejiaoyao1Mutant Is an Allele ofkorrigan1That Abolishes Endoglucanase Activity and Affects the Organization of Both Cellulose Microfibrils and Microtubules inArabidopsis

et al. 2014

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In higher plants, cellulose is synthesized by plasma membrane-localized cellulose synthase complexes (CSCs). Arabidopsis thaliana GH9A1/KORRIGAN1 is a membrane-bound, family 9 glycosyl hydrolase that is important for cellulose synthesis in both primary and secondary cell walls. Most previously identified korrigan1 mutants show severe phenotypes such as embryo lethality; therefore, the role of GH9A1 in cellulose synthesis remains unclear. Here, we report a novel A577V missense mutation, designated jiaoyao1 (jia1), in the second of the glycosyl hydrolase family 9 active site signature motifs in GH9A1. jia1 is defective in cell expansion in dark-grown hypocotyls, roots, and adult plants. Consistent with its defect in cell expansion, this mutation in GH9A1 resulted in reduced cellulose content and reduced CSC velocity at the plasma membrane. Green fluorescent protein-GH9A1 is associated with CSCs at multiple locations, including the plasma membrane, Golgi, trans-Golgi network, and small CESA-containing compartments or microtubuleassociated cellulose synthase compartments, indicating a tight association between GH9A1 and CSCs. GH9A1 A577V abolishes the endoglucanase activity of GH9A1 in vitro but does not affect its interaction with CESAs in vitro, suggesting that endoglucanase activity is important for cellulose synthesis. Interestingly, jia1 results in both cellulose microfibril and microtubule disorganization. Our study establishes the important role of endoglucanase in cellulose synthesis and cellulose microfibril organization in plants.

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“…The latter class can further be divided into two groups depending on whether or not these proteins contain a cellulose-binding domain (CBD) at the C-terminal. It has been previously reported that transmembrane EGs might be related to the biological synthesis of plant cellulose (Libertini et al 2004;Brummell et al 1997), and secreted…”

Section: Discussionmentioning

confidence: 99%

Expression of Two Endo-1,4-β-glucanase Genes During Fruit Ripening and Softening of Two Pear Varieties

Yang

Zhang

et al. 2016

FSTR

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A membrane-anchored E-type endo-1,4-β-glucanase is localized on Golgi and plasma membranes of higher plants

Cited by 126 publications

References 31 publications

AnArabidopsisEndo-1,4-β-d-Glucanase Involved in Cellulose Synthesis Undergoes Regulated Intracellular Cycling[W]

AnArabidopsisEndo-1,4-β-d-Glucanase Involved in Cellulose Synthesis Undergoes Regulated Intracellular Cycling[W]

Thejiaoyao1Mutant Is an Allele ofkorrigan1That Abolishes Endoglucanase Activity and Affects the Organization of Both Cellulose Microfibrils and Microtubules inArabidopsis

Expression of Two Endo-1,4-β-glucanase Genes During Fruit Ripening and Softening of Two Pear Varieties

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