Novel type <i>Arabidopsis thaliana</i> H<sup>+</sup>‐PPase is localized to the Golgi apparatus

Mitsuda, Nobutaka; Enami, Kazumasa; Nakata, Mami; Takeyasu, Kunio; Sato, Masa H.

doi:10.1016/s0014-5793(00)02400-5

Cited by 73 publications

(51 citation statements)

References 42 publications

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“…Like AtSAC1-GFP in Arabidopsis root cells, AtSAC1-enhanced yellow fluorescent protein (EYFP) and AtSAC1-enhanced cyan fluorescent protein (ECFP) displayed punctate localization patterns in carrot protoplasts ( Figure 9). It was found that the punctate pattern of AtSAC1-EYFP was almost identical to the localization pattern of the Golgi marker Arabidopsis proton-translocating pyrophosphatase2 (AVP2) (Figures 9A to 9D) (Mitsuda et al, 2001) but showed obvious differences from those of the prevacuolar membrane marker Ras-related small GTP binding protein1 (Rha1) (Figures 9E to 9H) (Lee et al, 2004) and an ER marker ( Figures 9I to 9L). These results suggest that AtSAC1 is associated with Golgi in the cells.…”

Section: Subcellular Localization Of the Atsac1 Proteinmentioning

confidence: 78%

Mutation of SAC1, an Arabidopsis SAC Domain Phosphoinositide Phosphatase, Causes Alterations in Cell Morphogenesis, Cell Wall Synthesis, and Actin Organization

et al. 2005

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SAC (for suppressor of actin) domain proteins in yeast and animals have been shown to modulate the levels of phosphoinositides, thereby regulating several cellular activities such as signal transduction, actin cytoskeleton organization, and vesicle trafficking. Nine genes encoding SAC domain-containing proteins are present in the Arabidopsis thaliana genome, but their roles in plant cellular functions and plant growth and development have not been characterized. In this report, we demonstrate the essential roles of one of the Arabidopsis SAC domain proteins, AtSAC1, in plant cellular functions. Mutation of the AtSAC1 gene in the fragile fiber7 (fra7) mutant caused a dramatic decrease in the wall thickness of fiber cells and vessel elements, thus resulting in a weak stem phenotype. The fra7 mutation also led to reduced length and aberrant shapes in fiber cells, pith cells, and trichomes and to an alteration in overall plant architecture. The AtSAC1 gene was found to be expressed in all tissues in elongating organs; however, it showed predominant expression in vascular tissues and fibers in nonelongating parts of stems. In vitro activity assay demonstrated that AtSAC1 exhibited phosphatase activity toward phosphatidylinositol 3,5-biphosphate. Subcellular localization studies showed that AtSAC1 was colocalized with a Golgi marker. Truncation of the C terminus by the fra7 mutation resulted in its localization in the cytoplasm but had no effect on phosphatase activity. Furthermore, examination of the cytoskeleton organization revealed that the fra7 mutation caused the formation of aberrant actin cables in elongating cells but had no effect on the organization of cortical microtubules. Together, these results provide genetic evidence that AtSAC1, a SAC domain phosphoinositide phosphatase, is required for normal cell morphogenesis, cell wall synthesis, and actin organization.

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Section: Subcellular Localization Of the Atsac1 Proteinmentioning

confidence: 78%

Mutation of SAC1, an Arabidopsis SAC Domain Phosphoinositide Phosphatase, Causes Alterations in Cell Morphogenesis, Cell Wall Synthesis, and Actin Organization

et al. 2005

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“…Interestingly, sugar-responsive cis-elements (i.e. AMY, BOX1 and -2 CGACG boxes) are present in the regulatory region of the AVP1 promoter (Mitsuda et al, 2001). Up-regulation of H + -PPase genes has been reported in Suc-starved cells of rice (Wang et al, 2007).…”

Section: The Sugar and Phosphate Connectionmentioning

confidence: 99%

Genetic Manipulation of a “Vacuolar” H+-PPase: From Salt Tolerance to Yield Enhancement under Phosphorus-Deficient Soils

et al. 2012

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“…TgM2AP⌬pro also overlapped with TgVP1, a "vacuolar" proton pyrophosphatase ( Figure 5D). Vacuolar proton pyrophosphatases acidify intracellular compartments, including digestive (Zhen et al, 1994) or contractile vacuoles (Montalvetti et al, 2004), acidocalcisomes (Montalvetti et al, 2004), or the trans-Golgi (Mitsuda et al, 2001) by using pyrophosphate hydrolysis to drive the translocation of protons across endomembranes.…”

Section: The Tgm2ap Propeptide Is Probably Not Required For Folding mentioning

confidence: 99%

A Cleavable Propeptide InfluencesToxoplasmaInfection by Facilitating the Trafficking and Secretion of the TgMIC2–M2AP Invasion Complex

Harper

Huynh

Coppens

et al. 2006

MBoC

101

150

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Propeptides regulate protein function and trafficking in many eukaryotic systems and have emerged as important features of regulated secretory proteins in parasites of the phylum Apicomplexa. Regulated protein secretion from micronemes and host cell invasion are inextricably linked and essential processes for the apicomplexan parasite Toxoplasma gondii. TgM2AP is a propeptide-containing microneme protein found in a heterohexameric complex with the microneme protein TgMIC2, a protein that has a demonstrated fundamental role in gliding motility and invasion. TgM2AP function is also central to these processes, because disruption of TgM2AP (m2apKO) results in secretory retention of TgMIC2, leading to reduced TgMIC2 secretion from the micronemes and impaired invasion. Because the TgM2AP propeptide is predicted to be processed in an intracellular site near where TgMIC2 is retained in m2apKO parasites, we hypothesized that the propeptide and its proteolytic removal influence trafficking and secretion of the complex. We found that proTgM2AP traffics through endosomal compartments and that deletion of the propeptide leads to defective trafficking of the complex within or near this site, resulting in aberrant processing and decreased secretion of TgMIC2, impaired invasion, and reduced virulence in vivo, mirroring the phenotypes observed in m2apKO parasites. In contrast, mutation of several cleavage site residues resulted in normal localization, but it affected the stability and secretion of the complex from the micronemes. Therefore, the propeptide and its cleavage site influence distinct aspects of TgMIC2-M2AP function, with both impacting the outcome of infection. INTRODUCTIONEukaryotic secretory proteins use an assortment of luminal or cytoplasmic forward targeting signals to navigate the secretory system for eventual delivery to the extracellular environment. Among the least well understood of the luminal signals are cleavable elements known as propeptides, which are typically positioned either internally or, more commonly, at the N terminus of a protein. Propeptides have been shown to serve in several capacities. They can facilitate the folding of their cognate protein, regulate its activity or oligomeric assembly, or direct it to a particular intracellular compartment within the endolysosomal or secretory system. For proproteins destined for the regulated secretory pathway, proteolytic processing (also termed proteolytic maturation) typically accompanies the condensation of immature secretory granule contents (Orci et al., 1987;Kuiper and Martens, 2000). Yet, the precise role of proteolytic maturation in the biogenesis and discharge of regulated secretory organelles remains contentious (Arvan and Halban, 2004).Toxoplasma gondii, the etiological agent of toxoplasmosis, is a genetically tractable protozoan parasite that causes widespread infection in humans resulting in significant economic losses worldwide (Jones et al., 2001). As a member of the phylum Apicomplexa, T. gondii features a distinct apical complex consis...

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Novel type Arabidopsis thaliana H⁺‐PPase is localized to the Golgi apparatus

Cited by 73 publications

References 42 publications

Mutation of SAC1, an Arabidopsis SAC Domain Phosphoinositide Phosphatase, Causes Alterations in Cell Morphogenesis, Cell Wall Synthesis, and Actin Organization

Mutation of SAC1, an Arabidopsis SAC Domain Phosphoinositide Phosphatase, Causes Alterations in Cell Morphogenesis, Cell Wall Synthesis, and Actin Organization

Genetic Manipulation of a “Vacuolar” H+-PPase: From Salt Tolerance to Yield Enhancement under Phosphorus-Deficient Soils

A Cleavable Propeptide InfluencesToxoplasmaInfection by Facilitating the Trafficking and Secretion of the TgMIC2–M2AP Invasion Complex

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Novel type Arabidopsis thaliana H+‐PPase is localized to the Golgi apparatus

Cited by 73 publications

References 42 publications

Mutation of SAC1, an Arabidopsis SAC Domain Phosphoinositide Phosphatase, Causes Alterations in Cell Morphogenesis, Cell Wall Synthesis, and Actin Organization

Mutation of SAC1, an Arabidopsis SAC Domain Phosphoinositide Phosphatase, Causes Alterations in Cell Morphogenesis, Cell Wall Synthesis, and Actin Organization

Genetic Manipulation of a “Vacuolar” H+-PPase: From Salt Tolerance to Yield Enhancement under Phosphorus-Deficient Soils

A Cleavable Propeptide InfluencesToxoplasmaInfection by Facilitating the Trafficking and Secretion of the TgMIC2–M2AP Invasion Complex

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Novel type Arabidopsis thaliana H⁺‐PPase is localized to the Golgi apparatus