Interaction between Aldolase and Vacuolar H+-ATPase

Lu, Ming; Holliday, L. Shannon; Zhang, Li; Dunn, William A.; Gluck, Stephen L.

doi:10.1074/jbc.m008768200

Cited by 173 publications

(98 citation statements)

References 48 publications

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“…However, recent cross-linking experiments have suggested that the Esubunit occupies a peripheral position (58). Such an exposed position agrees with several regulatory protein-protein interactions described for the E-subunit (59,60). Accordingly, the central stalk is probably formed by the D-subunit, which is essential for coupling proton transport and ATP hydrolysis (61), and the F-subunit, which is in close proximity to the 2 The atomic coordinates of the A1C12 subcomplex of D-subunit (62,63).…”

Section: Discussionsupporting

confidence: 61%

Three-dimensional Map of a Plant V-ATPase Based on Electron Microscopy

Domgall

Venzke

Lüttge

et al. 2002

Journal of Biological Chemistry

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V-ATPases pump protons into the interior of various subcellular compartments at the expense of ATP. Previous studies have shown that these pumps comprise a membrane-integrated, proton-translocating (V 0 ), and a soluble catalytic (V 1 ) subcomplex connected to one another by a thin stalk region. We present two three-dimensional maps derived from electron microscopic images of the complete V-ATPase complex from the plant Kalanchoë daigremontiana at a resolution of 2.2 nm. In the presence of a non-hydrolyzable ATP analogue, the details of the stalk region between V 0 and V 1 were revealed for the first time in their three-dimensional organization. A central stalk was surrounded by three peripheral stalks of different sizes and shapes. In the absence of the ATP analogue, the tilt of V 0 changed with respect to V 1 , and the stalk region was less clearly defined, perhaps due to increased flexibility and partial detachment of some of the peripheral stalks. These structural changes corresponded to decreased stability of the complex and might be the initial step in a controlled disassembly. V-ATPases1 are found in all eukaryotic cells. They hydrolyze ATP to pump protons into various intracellular compartments (1). In plant tonoplasts the proton motive force generated by the V-ATPase is used for secondary transport processes contributing to osmoregulation, ion and pH homeostasis, nutrient and remnant storage, and plant defense (2).V-ATPases are highly conserved among species, and their gross architecture is similar to that of the well characterized F-ATPases. In the V-ATPases, the soluble V 1 subcomplex is known to carry the catalytic nucleotide-binding sites and to be connected via a thinner stalk region to the membrane-integrated V 0 subcomplex, which contains the proton-translocating machinery. The exact subunit composition and stoichiometry of V-ATPases, however, is still controversial. In yeast, the V 1 subcomplex is probably formed by the subunits (AB) 3 , C-H, and the V 0 subcomplex by the subunits c, cЈ, cЉ, a, and d (for review see Ref.3). Homologues of the cЈ-and cЉ-subunits have not been identified in plants as of yet (4).Among the subunits known to comprise V-ATPases, several share significant sequence homology to subunits of F-ATPases.The catalytic A-subunits of V-ATPase are homologous to the catalytic ␤-subunits in F-ATPase (5) and the B-subunits of V-ATPase to the non-catalytic ␣-subunits in F-ATPase (6). The membrane-integrated V-ATPase c-subunit has probably emerged by gene duplication (7) from a common ancestor of Fand V-ATPases. The G-subunit of V-ATPases has sequence similarity to the hydrophilic part of the membrane-anchored F-ATPase b-subunit (8). Other components of the F-ATPase machinery do not have any homologues in V-ATPase. Furthermore, V-ATPases contain various subunits (C, F, H, a, and d) whose functions and relationships to F-ATPases still need to be elucidated. This divergence might reflect an adaptation to the different physiological requirements of F-and V-ATPases. Unlike F-ATPases, V-AT...

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Section: Discussionsupporting

confidence: 61%

Three-dimensional Map of a Plant V-ATPase Based on Electron Microscopy

Domgall

Venzke

Lüttge

et al. 2002

Journal of Biological Chemistry

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“…Processing of the positive clones was performed as described (13). The selected two-hybrid colonies were grown overnight in yeast/peptone/dextrose medium to stationary phase in polypropylene tubes.…”

Section: Methodsmentioning

confidence: 99%

Section: Expression Of the Amino-terminal Domain Of The E Subunit Resmentioning

confidence: 99%

“…The glycolytic enzyme aldolase interacts in vitro and in vivo with the E subunit of V-ATPase (13). Upon immunofluorescent staining, aldolase co-localizes extensively with V-ATPase both in the kidney proximal tubule and in the osteoclast (13). In osteoclasts, cells that are essential for bone remodeling, aldolase undergoes a subcellular redistribution from cytoplasmic vesicles to the ruffled membrane together with V-ATPase following osteoclast activation (13).…”

Section: Expression Of the Amino-terminal Domain Of The E Subunit Resmentioning

confidence: 99%

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The Amino-terminal Domain of the E Subunit of Vacuolar H+-ATPase (V-ATPase) Interacts with the H Subunit and Is Required for V-ATPase Function

Lu¹,

Vergara²,

Zhang³

et al. 2002

Journal of Biological Chemistry

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Vacuolar H؉ -ATPases (V-ATPases) are highly conserved proton pumps that couple hydrolysis of cytosolic ATP to proton transport out of the cytosol. Although it is generally believed that V-ATPases transport protons by a rotary catalytic mechanism analogous to that used by F 1 F 0 -ATPases, the structure and subunit composition of the central or peripheral stalk of the multisubunit complex are not well understood. We searched for proteins that bind to the E subunit of V-ATPase using the yeast two-hybrid assay and identified the H subunit as an interacting partner. Physical association between the E and H subunits of V-ATPase was confirmed in vitro by precipitation assays. Deletion mapping analysis revealed that a 78-amino acid fragment at the amino terminus of the E subunit was sufficient for binding to the H subunit. Expression of the amino-terminal fragments of the E subunits from human and yeast as dominantnegative mutants resulted in dramatic decreases in bafilomycin A 1 -sensitive ATP hydrolysis and proton transport activities of V-ATPase. Our data demonstrate the physiological significance of the interaction between the E and H subunits of V-ATPase and extend previous studies on the arrangement of subunits on the peripheral stalk of V-ATPase. Vacuolar Hϩ -ATPases (V-ATPases) 1 energize and acidify intracellular compartments of the vacuolar system of eukaryotic cells. They are essential for the normal function of secretory vesicles, the trans-Golgi network, endosomes, lysosomes, the yeast vacuole, and other intracellular membrane compartments (1, 2). In some specialized cells such as the intercalated cells of the kidney and the osteoclasts, V-ATPases reside at high levels on the plasma membrane, where they are responsible for transepithelial or cellular proton transport required for normal acid-base homeostasis and bone remodeling (2). Despite their wide range of physiological functions, V-ATPases share a highly conserved structure and common enzymatic properties that couple hydrolysis of cytosolic ATP to proton transport out of the cytosol (3). They contain two macrodomains or sectors: V 1 , a catalytic domain composed of peripheral membrane proteins, and V 0 , a transmembrane domain composed of intrinsic membrane proteins that transmits protons through the lipid bilayer (4). The V 1 domain attaches to the V 0 domain at the cytoplasmic face of the membrane. In Saccharomyces cerevisiae, the V 1 domain is composed of eight distinct polypeptide chains, and the V 0 domain contains five (4).V-ATPases are evolutionarily related and structurally similar to F 1 F 0 -ATPases (F-ATPases) of bacteria, chloroplasts, and mitochondria (3). F-ATPases also have two sectors: F 1 , a peripherally attached complex composed of a catalytic head and a stalk, and F 0 , composed of intrinsic membrane subunits and a stator arm. F-ATPases have a rotary catalytic mechanism (5-7). The proton electrochemical gradient across the membrane drives translocation of protons through a pathway composed of the a and c subunits in the F 0 sector,...

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“…In animal cells studies have paid special attention to the spatial organization of glycolysis, because the physical concentrations of glycolytic enzymes may be associated with sites with high demand for ATP (Lu et al, 2001;Giegé et al, 2003) or other intermediates of glycolysis (Giegé et al, 2003;Fernie et al, 2004). A study in Arabidopsis established that the enzymes HXK, GADPH, and phosphofructokinase (PFK) were functionally associated with mitochondria (Giegé et al, 2003).…”

Section: Glycolysis In Plantsmentioning

confidence: 99%

Plant respiration under low oxygen

Toro¹,

Pinto

2015

Chilean J. Agric. Res.

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Respiration is an oxidative process controlled by three pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and oxidative phosphorylation (OXPHOS). Respiratory metabolism is ubiquitous in all organisms, but with differences among each other. For example in plants, because their high plasticity, respiration involves metabolic pathways with unique characteristics. In this way, in order to avoid states of low energy availability, plants exhibit great flexibility to bypass conventional steps of glycolysis, TCA cycle, and OXPHOS. To understand the energetic link between these alternative pathways, it is important to know the growth, maintenance, and ion uptake components of the respiration in plants. Changes in these components have been reported when plants are subjected to stress, such as oxygen deficiency. This review analyzes the current knowledge on the metabolic and functional aspects of plant respiration, its components and its response to environmental changes.

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Interaction between Aldolase and Vacuolar H+-ATPase

Cited by 173 publications

References 48 publications

Three-dimensional Map of a Plant V-ATPase Based on Electron Microscopy

Three-dimensional Map of a Plant V-ATPase Based on Electron Microscopy

The Amino-terminal Domain of the E Subunit of Vacuolar H+-ATPase (V-ATPase) Interacts with the H Subunit and Is Required for V-ATPase Function

Plant respiration under low oxygen

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