Activation of H+-ATPase by glucose in Saccharomyces cerevisiae involves a membrane serine protease

Campetelli, Alexis N.; Monesterolo, Noelia E.; Previtali, Gabriela; Santander, Verónica S.; Amaiden, Marina R.; Arce, Carlos A.; Taubas, Javier Valdez; Casale, César H.

doi:10.1016/j.bbagen.2013.03.012

Cited by 11 publications

(6 citation statements)

References 41 publications

(59 reference statements)

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“…Stabilization of the autoinhibited state of PM H + ‐ATPase may require association with other proteins. Indeed, acetylated tubulin has been shown to interact with Pma1p in the basal state only and the addition of acetylated tubulin can even inactivate Pma1p in vitro . We therefore expected that acetylated tubulin would co‐purify with Pma1p in its basal state.…”

Section: Discussionmentioning

confidence: 99%

“…1A). As it has been reported that acetylated tubulin is essential for keeping Pma1p in the basal state [22,23], we tested whether one of the contaminating proteins was acetylated tubulin. The anti-acetylated tubulin antibody only decorated a band in the PM fractions and in the nonsolubilized material, but was absent from the purified fraction (Fig.…”

Section: Absence Of Acetylated Tubulin In Purified Pma1p Preparationmentioning

confidence: 99%

“…It has been reported that Pma1p interacts with acetylated tubulin, which may stabilize the pump in its basal state [22]. A mechanism has also been proposed according to which glucose sensing leads to activation of a serine protease, that in turn causes hydrolysis of acetylated tubulin and its dissociation from the pump, thereby forcing Pma1p into the activated state [23].…”

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confidence: 99%

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Isolation of native plasma membrane H⁺‐ATPase (Pma1p) in both the active and basal activation states

et al. 2018

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The yeast plasma membrane H + ‐ ATP ase Pma1p is a P‐type ATP ase that energizes the yeast plasma membrane. Pma1p exists in two activation states: an autoinhibited basal state and an activated state. Here we show that functional and stable Pma1p can be purified in native form and reconstituted in artificial liposomes without altering its activation state. Acetylated tubulin has previously been reported to maintain Pma1p in the basal state but, as this protein was absent from the purified preparations, it cannot be an essential component of the autoinhibitory mechanism. Purification of and reconstitution of native Pma1p in both activation states opens up for a direct comparison of the transport properties of these states, which allowed us to confirm that the basal state has a low coupling ratio between ATP hydrolysis and protons pumped, whereas the activated state has a high coupling ratio. The ability to prepare native Pma1p in both activation states will facilitate further structural and biochemical studies examining the mechanism by which plasma membrane H + ‐ ATP ases are autoinhibited.

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Section: Discussionmentioning

confidence: 99%

Section: Absence Of Acetylated Tubulin In Purified Pma1p Preparationmentioning

confidence: 99%

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Isolation of native plasma membrane H⁺‐ATPase (Pma1p) in both the active and basal activation states

et al. 2018

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“…In the following 5 years, it was demonstrated that the interaction between tubulin and NKA regulates NKA activity in different types of cell, and that this interaction has an important physiological role (Casale et al, , ). These findings highlighted a new mechanism for the regulation of NKA activity: The reversible tubulin–NKA interaction, which was then extended to other P‐ATPases such as PMCA and H + ‐ATPase (Arce, Casale, & Barra, ; Campetelli et al, ; Campetelli, Previtali, Arce, Barra, & Casale, ; Monesterolo et al, , ).…”

Section: Introductionmentioning

confidence: 87%

“…The reversible tubulin-NKA interaction, which was then extended to other P-ATPases such as PMCA and H + -ATPase Campetelli et al, 2013;Campetelli, Previtali, Arce, Barra, & Casale, 2005;Monesterolo et al, 2008Monesterolo et al, , 2012. Tubulin is formed by two different polypeptides (α and β) and each of them is codified by several genes.…”

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Tubulin–Na⁺_,K⁺‐ATPase interaction: Involvement in enzymatic regulation and cellular function

Santander

Campetelli

Monesterolo

et al. 2018

Journal Cellular Physiology

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A new function for tubulin was described by our laboratory: acetylated tubulin forms a complex with Na+,K +‐ATPase (NKA) and inhibits its activity. This process was shown to be a regulatory factor of physiological importance in cultured cells, human erythrocytes, and several rat tissues. Formation of the acetylated tubulin–NKA complex is reversible. We demonstrated that in cultured cells, high concentrations of glucose induce translocation of acetylated tubulin from cytoplasm to plasma membrane with a consequent inhibition of NKA activity. This effect is reversed by adding glutamate, which is coctransported to the cell with Na +. Another posttranslational modification of tubulin, detyrosinated tubulin, is also involved in the regulation of NKA activity: it enhances the NKA inhibition induced by acetylated tubulin. Manipulation of the content of these modifications of tubulin could work as a new strategy to maintain homeostasis of Na + and K +, and to regulate a variety of functions in which NKA is involved, such as osmotic fragility and deformability of human erythrocytes. The results summarized in this review show that the interaction between tubulin and NKA plays an important role in cellular physiology, both in the regulation of Na +/K + homeostasis and in the rheological properties of the cells, which is mechanically different from other roles reported up to now.

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Serine Proteases as Metabolic Regulators in Yeast

Campetelli

Monesterolo

2017

Pathophysiological Aspects of Proteases

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Activation of H+-ATPase by glucose in Saccharomyces cerevisiae involves a membrane serine protease

Cited by 11 publications

References 41 publications

Isolation of native plasma membrane H⁺‐ATPase (Pma1p) in both the active and basal activation states

Isolation of native plasma membrane H⁺‐ATPase (Pma1p) in both the active and basal activation states

Tubulin–Na⁺_,K⁺‐ATPase interaction: Involvement in enzymatic regulation and cellular function

Serine Proteases as Metabolic Regulators in Yeast

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Activation of H+-ATPase by glucose in Saccharomyces cerevisiae involves a membrane serine protease

Cited by 11 publications

References 41 publications

Isolation of native plasma membrane H+‐ATPase (Pma1p) in both the active and basal activation states

Isolation of native plasma membrane H+‐ATPase (Pma1p) in both the active and basal activation states

Tubulin–Na+,K+‐ATPase interaction: Involvement in enzymatic regulation and cellular function

Serine Proteases as Metabolic Regulators in Yeast

Contact Info

Product

Resources

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Isolation of native plasma membrane H⁺‐ATPase (Pma1p) in both the active and basal activation states

Isolation of native plasma membrane H⁺‐ATPase (Pma1p) in both the active and basal activation states

Tubulin–Na⁺_,K⁺‐ATPase interaction: Involvement in enzymatic regulation and cellular function