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Plant Ca2+-ATPases: From biochemistry to signalling.
Costa, Alex; Resentini, Francesca; Buratti, Stefano; Bonza, Maria Cristina.
Affiliation
  • Costa A; Department of Biosciences, University of Milan, via Celoria 26, 20133 Milano, Italy; Institute of Biophysics, National Research Council of Italy (CNR), 20133 Milano, Italy. Electronic address: alex.costa@unimi.it.
  • Resentini F; Department of Biosciences, University of Milan, via Celoria 26, 20133 Milano, Italy.
  • Buratti S; Department of Biosciences, University of Milan, via Celoria 26, 20133 Milano, Italy. Electronic address: stefano.buratti@unimi.it.
  • Bonza MC; Department of Biosciences, University of Milan, via Celoria 26, 20133 Milano, Italy. Electronic address: cristina.bonza@unimi.it.
Biochim Biophys Acta Mol Cell Res ; 1870(7): 119508, 2023 10.
Article in En | MEDLINE | ID: mdl-37290725
ABSTRACT
Calcium (Ca2+)-ATPases are ATP-dependent enzymes that transport Ca2+ ions against their electrochemical gradient playing the fundamental biological function of keeping the free cytosolic Ca2+ concentration in the submicromolar range to prevent cytotoxic effects. In plants, type IIB autoinhibited Ca2+-ATPases (ACAs) are localised both at the plasma membrane and at the endomembranes including endoplasmic reticulum (ER) and tonoplast and their activity is primarily regulated by Ca2+-dependent mechanisms. Instead, type IIA ER-type Ca2+-ATPases (ECAs) are present mainly at the ER and Golgi Apparatus membranes and are active at resting Ca2+. Whereas research in plants has historically focused on the biochemical characterization of these pumps, more recently the attention has been also addressed on the physiological roles played by the different isoforms. This review aims to highlight the main biochemical properties of both type IIB and type IIA Ca2+ pumps and their involvement in the shaping of cellular Ca2+ dynamics induced by different stimuli.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Calcium-Transporting ATPases / Adenosine Triphosphatases Language: En Journal: Biochim Biophys Acta Mol Cell Res Year: 2023 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Calcium-Transporting ATPases / Adenosine Triphosphatases Language: En Journal: Biochim Biophys Acta Mol Cell Res Year: 2023 Document type: Article