Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons

Robinson, David G.; Haschke, Hans-Peter; Hinz, Giselbert; Hoh, Birgit; Maeshima, Masayoshi; Marty, Francis

doi:10.1007/bf00197591

Cited by 88 publications

(67 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, immunocytochemical tests indicated that these V-ATPase subunits occur on the plasma-(as well as the vacuolar) membrane. This finding was confirmed independently by Robinson's group in Gottingen, Germany (13).…”

Section: Isolationsupporting

confidence: 53%

Enzymology and Molecular Biology of Cell Wall Biosynthesis. Final Technical Report

Ray¹

2000

View full text Add to dashboard Cite

Section: Isolationsupporting

confidence: 53%

Enzymology and Molecular Biology of Cell Wall Biosynthesis. Final Technical Report

Ray¹

2000

View full text Add to dashboard Cite

“…Moreover, although several proteins have been identified as mitochondrial or vacuolar, there is evidence that some of these (e.g. ATP synthases [Bae et al, 2004], voltage-dependent anion channels [Bathori et al, 1999], or V-type ATPases [Robinson et al, 1996;Rouquie et al, 1998]) may also have a PM localization. Surprisingly we found a high diversity of ribosomal proteins in the M. truncatula DIM fraction (Table V), similar to a previous study on the Arabidopsis PM (Alexandersson et al, 2004).…”

Section: Proteomic Approach Of the Protein Content Of M Truncatula Rmentioning

confidence: 99%

Characterization of Lipid Rafts from Medicago truncatula Root Plasma Membranes: A Proteomic Study Reveals the Presence of a Raft-Associated Redox System

Furt²,

et al. 2007

View full text Add to dashboard Cite

Several studies have provided new insights into the role of sphingolipid/sterol-rich domains so-called lipid rafts of the plasma membrane (PM) from mammalian cells, and more recently from leaves, cell cultures, and seedlings of higher plants. Here we show that lipid raft domains, defined as Triton X-100-insoluble membranes, can also be prepared from Medicago truncatula root PMs. These domains have been extensively characterized by ultrastructural studies as well as by analysis of their content in lipids and proteins. M. truncatula lipid domains are shown to be enriched in sphingolipids and D 7 -sterols, with spinasterol as the major compound, but also in steryl glycosides and acyl-steryl glycosides. A large number of proteins (i.e. 270) have been identified. Among them, receptor kinases and proteins related to signaling, cellular trafficking, and cell wall functioning were well represented whereas those involved in transport and metabolism were poorly represented. Evidence is also given for the presence of a complete PM redox system in the lipid rafts.

show abstract

“…Second, the distribution of V-ATPase activity in diverse plant endomembranes indicates that their essentiality extends beyond the roles of the central vacuole . V-ATPase activity or protein has been demonstrated in membranes from young roots lacking large central vacuoles (Herman et al, 1994), in Golgi of suspension-cultured cells (Ali and Akazawa, 1986), and in the plasma membrane (Robinson et al, 1996). Fluorescence-labeled antibodies against subunit B or green fluorescent protein-tagged subunit C stained the perinuclear region of root tips (Schumacher et al, 1999), and immuno-electron microscopy demonstrated that V-ATPase was associated with the ER and small vacuoles or vesicles (Herman et al, 1994).…”

Section: Role Of V-atpase In Vesicular Traffic: a Modelmentioning

confidence: 99%

Differential Expression of Vacuolar H+-ATPase Subunit c Genes in Tissues Active in Membrane Trafficking and Their Roles in Plant Growth as Revealed by RNAi

et al. 2004

View full text Add to dashboard Cite

Acidification of intracellular compartments by the vacuolar-type H1 -ATPases (VHA) is known to energize ion and metabolite transport, though cellular processes influenced by this activity are poorly understood. At least 26 VHA genes encode 12 subunits of the V 1 V o -ATPase complex in Arabidopsis, and how the expression, assembly, and activity of the pump are integrated into signaling networks that govern growth and adaptation are largely unknown. The role of multiple VHA-c genes encoding the 16-kD subunit of the membrane V o sector was investigated. Expression of VHA-c1, monitored by promoter-driven b-glucuronidase (GUS) activity was responsive to light or dark in an organ-specific manner. VHA-c1 expression in expanding cotyledons, hypocotyls of etiolated seedlings, and elongation zone of roots supported a role for V-ATPase in cell enlargement. Mutants reduced in VHA-c1 transcript using dsRNA-mediated interference showed reduction in root growth relative to wildtype seedlings. In contrast, VHA-c3 promoter::GUS expression was undetectable in most organs of seedlings, but strong in the root cap. Interestingly, dsRNA-mediated mutants of vha-c3 also showed reduced root length and decreased tolerance to moderate salt stress. The results suggest that V-ATPase functions in the root cap influenced root growth. Expression of VHA-c1 and VHA-c3 in tissues with active membrane flow, including root cap, vascular strands, and floral style would support a model for participation of the V o sector and V 1 V o -ATPase in membrane trafficking and fusion. Two VHA-c genes are thus differentially expressed to support growth in expanding cells and to supply increased demand for V-ATPase in cells with active exocytosis.From the perspective of physiologists and biochemists, it is well established that primary proton pumps are crucial for plant growth and survival. Among three distinct proton pumps, the most complex is the vacuolar-type H 1 -ATPase. Physiological and biochemical studies have demonstrated that acidification of the vacuolar compartment by this pump energizes the uptake and release of ions and metabolites (Sze et al., 1992;Lü ttge and Ratajczak, 1997). However, due to its structural complexity, we know very little about how the expression, assembly, and activity of this pump are integrated into the signaling networks that govern the life cycle of plants. In addition to its association with vacuolar membranes in plant cells, the pump has been localized to diverse subcellular membranes, including the Golgi (Ali and Akazawa, 1986; Matsuoka et al., 1997), endoplasmic reticulum (ER; Herman et al., 1994), intracellular vesicles, and the plasma membrane Schumacher et al., 1999;Dietz et al., 2001). Yet the specific subcellular functions of V-ATPases in distinct cell types and their consequences on a developing multicellular plant are largely unknown. Thus, from the perspectives of molecular, cell, and developmental biologists, many questions remain.Based on extensive biochemical and structural studies from animal, yeast and plant...

show abstract

Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons

Cited by 88 publications

References 49 publications

Enzymology and Molecular Biology of Cell Wall Biosynthesis. Final Technical Report

Enzymology and Molecular Biology of Cell Wall Biosynthesis. Final Technical Report

Characterization of Lipid Rafts from Medicago truncatula Root Plasma Membranes: A Proteomic Study Reveals the Presence of a Raft-Associated Redox System

Differential Expression of Vacuolar H+-ATPase Subunit c Genes in Tissues Active in Membrane Trafficking and Their Roles in Plant Growth as Revealed by RNAi

Contact Info

Product

Resources

About