Ca<sup>2+</sup>-Translocating ATPase of the Plant Plasma Membrane

Briskin, Donald P.

doi:10.1104/pp.94.2.397

Cited by 94 publications

(72 citation statements)

References 10 publications

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“…The 111-kD polypeptide in the present investigation was identified as a Ca 2+ -ATPase by its ability to form a Ca 2 " 1 "-dependent, hydroxylamine-sensitive phosphorylated intermediate in the presence of [y-32 P]ATP ( Fig. 2; Briskin, 1990;Garrahan and Rega, 1990). The amount of phosphorylated intermediate of the partly purified Ca 2+ -ATPase increased in the presence of La 3+ (Fig.…”

Section: Purification Of Ca 2+ -Atpase From Low-density Membranesmentioning

confidence: 99%

Modulation of an Intracellular Calmodulin-Stimulated Ca2+-Pumping ATPase in Cauliflower by Trypsin (The Use of Calcium Green-5N to Measure Ca2+ Transport in Membrane Vesicles)

Askerlund

1996

Plant Physiol.

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The effect of controlled trypsin digestion of a calmodulin-stimulated CaZ+-ATPase in low-density intracellular membranes from cauliflower (Brassica oleracea L.) inflorescences was investigated. CaZ+ uptake into vesicles was measured either continuously with the fluorescent Ca2+ indicator Calcium Creen-5N or with a radioactive filter technique. Trypsin treatment of vesicles resulted in a 3-fold activation of Ca2+ uptake and loss of calmodulin sensitivity. lmmunoblotting experiments with an antiserum raised against the CaZ+-ATPase showed that the trypsin activation was accompanied by a decrease in the amount of intact CaZ+-ATPase (1 1 1 kD) and by successive appearances of polypeptides of 102 and 99 to 84 kD. 'z51-Calmodulin overlays showed that only the intact Ca2+-ATPase bound calmodulin. Removal of the calmodulin-binding domain (about 9 kD) was not enough to obtain full activation. Trypsin proteolysis resulted in a Caz+ concentration necessary for halfmaximal activity of 0.5 p~, whereas a value of about 2 p~ was obtained with untreated membranes in the presence of calmodulin. Without trypsin treatment or calmodulin the activity was not saturated even at 57 JLM free CaZ+. The data suggest that trypsin digestion and calmodulin activate the cauliflower Ca2+-ATPase by at least partly different mechanisms.

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Section: Purification Of Ca 2+ -Atpase From Low-density Membranesmentioning

confidence: 99%

Modulation of an Intracellular Calmodulin-Stimulated Ca2+-Pumping ATPase in Cauliflower by Trypsin (The Use of Calcium Green-5N to Measure Ca2+ Transport in Membrane Vesicles)

Askerlund

1996

Plant Physiol.

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“…In plant cells, two types of transporters have been identified: highaffinity Ca2+-ATPases localized in the endoplasmic reticulum (ER), plasma membrane (PM), and tonoplast (TN), and a lower affinity Ca2+/H+ antiport localized in the vacuolar membranes (Evans et al, 1991;Chanson, 1993). Although the plant cell vacuolar Ca2+/H+ antiport is likely to play an important role in high-capacity intracellular storage, high-affinity Ca2+-ATPase-driven Caz+ transport has been proposed to play the most significant role in modulating cytosolic Ca2+ levels in the physiological range (Carafoli, 1987;Briskin, 1990).…”

Section: Introductionmentioning

confidence: 99%

A Single Gene May Encode Differentially Localized Ca 2+ -ATPases in Tomato

Ferrol¹,

Bennett²

1996

The Plant Cell

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Previously, a partial-length cDNA and a complete genomic clone encoding a putative sarcoplasmic reticulum-type Ca2+-ATPase (LCA, Lycopersicon _CaZ+-.ATPase) were isolated from tomato. To determine the subcellular localization of this Ca2+-ATPase, specific polyclonal antibodies raised against a fusion protein encoding a portion of the LCA polypeptide were generated. Based on hybridization of the LCA cDNA and of the nucleotide sequence encoding the fusion protein to genomic DNA, it appears that LCA and the fusion protein domain are encoded by a single gene in tomato. Antibodies raised against the LCA domain fusion protein reacted specifically with two polypeptides of 116 and 120 kD that are localized in the vacuolar and plasma membranes, respectively. The distribution of vanadate-sensitive ATP-dependent Ca2+ transport activities in sucrose gradients coincided with the distribution of the immunodetected proteins. The ATPdependent Ca2+ transport activities associated with tonoplast and plasma membrane fractions shared similar properties, because both fractions were inhibited by vanadate but insensitive to carbonyl cyanide m-chlorophenylhydrazone, nitrate, and calmodulin. Moreover, antibodies raised against the LCA domain fusion protein inhibited ATP-dependent Ca2+ uptake activity associated with both the tonoplast and plasma membrane fractions. These data suggest that a single gene (LCA) may encode two P-type Ca2+-ATPase isoforms that are differentially localized in the tonoplast and plasma membrane of tomato roots.

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“…a signal-induced increase of its concentration (reviewed by Briskin, 1990;Evans et al, 1991;De Michelis et al, 1992;Evans, 1994). The PM Ca2+-ATPase catalyzes a nH+t/Ca2+ antiport and so utilizes, besides the energy of hydrolysis of ATP, the proton electrochemical gradient built up by the PM H+-ATPase.…”

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confidence: 99%

Identification of the Plasma Membrane Ca2+-ATPase and of Its Autoinhibitory Domain

Rasi‐Caldogno¹,

Carnelli²,

Michelis³

1995

Plant Physiol.

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Ca²⁺-Translocating ATPase of the Plant Plasma Membrane

Cited by 94 publications

References 10 publications

Modulation of an Intracellular Calmodulin-Stimulated Ca2+-Pumping ATPase in Cauliflower by Trypsin (The Use of Calcium Green-5N to Measure Ca2+ Transport in Membrane Vesicles)

Modulation of an Intracellular Calmodulin-Stimulated Ca2+-Pumping ATPase in Cauliflower by Trypsin (The Use of Calcium Green-5N to Measure Ca2+ Transport in Membrane Vesicles)

A Single Gene May Encode Differentially Localized Ca 2+ -ATPases in Tomato

Identification of the Plasma Membrane Ca2+-ATPase and of Its Autoinhibitory Domain

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Ca2+-Translocating ATPase of the Plant Plasma Membrane

Cited by 94 publications

References 10 publications

Modulation of an Intracellular Calmodulin-Stimulated Ca2+-Pumping ATPase in Cauliflower by Trypsin (The Use of Calcium Green-5N to Measure Ca2+ Transport in Membrane Vesicles)

Modulation of an Intracellular Calmodulin-Stimulated Ca2+-Pumping ATPase in Cauliflower by Trypsin (The Use of Calcium Green-5N to Measure Ca2+ Transport in Membrane Vesicles)

A Single Gene May Encode Differentially Localized Ca 2+ -ATPases in Tomato

Identification of the Plasma Membrane Ca2+-ATPase and of Its Autoinhibitory Domain

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Ca²⁺-Translocating ATPase of the Plant Plasma Membrane