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      Structure and Mechanism of P-Type ATPase Ion Pumps

      Author(s): 1 , 2 , 1 , 2 , 1 , 2 , 1 , 2
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      Journal: Annual Review of Biochemistry
      Publisher: Annual Reviews

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          Abstract

          P-type ATPases are found in all kingdoms of life and constitute a wide range of cation transporters, primarily for H +, Na +, K +, Ca 2+, and transition metal ions such as Cu(I), Zn(II), and Cd(II). They have been studied through a wide range of techniques, and research has gained very significant insight on their transport mechanism and regulation. Here, we review the structure, function, and dynamics of P2-ATPases including Ca 2+-ATPases and Na,K-ATPase. We highlight mechanisms of functional transitions that are associated with ion exchange on either side of the membrane and how the functional cycle is regulated by interaction partners, autoregulatory domains, and off-cycle states. Finally, we discuss future perspectives based on emerging techniques and insights.

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          Sarcolipin is a newly identified regulator of muscle-based thermogenesis in mammals.

          Naresh Bal, Santosh Maurya, Danesh Sopariwala … (2012)
          The role of skeletal muscle in nonshivering thermogenesis (NST) is not well understood. Here we show that sarcolipin (Sln), a newly identified regulator of the sarco/endoplasmic reticulum Ca(2+)-ATPase (Serca) pump, is necessary for muscle-based thermogenesis. When challenged to acute cold (4 °C), Sln(-/-) mice were not able to maintain their core body temperature (37 °C) and developed hypothermia. Surgical ablation of brown adipose tissue and functional knockdown of Ucp1 allowed us to highlight the role of muscle in NST. Overexpression of Sln in the Sln-null background fully restored muscle-based thermogenesis, suggesting that Sln is the basis for Serca-mediated heat production. We show that ryanodine receptor 1 (Ryr1)-mediated Ca(2+) leak is an important mechanism for Serca-activated heat generation. Here we present data to suggest that Sln can continue to interact with Serca in the presence of Ca(2+), which can promote uncoupling of the Serca pump and cause futile cycling. We further show that loss of Sln predisposes mice to diet-induced obesity, which suggests that Sln-mediated NST is recruited during metabolic overload. These data collectively suggest that SLN is an important mediator of muscle thermogenesis and whole-body energy metabolism.
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            Modulation of cardiac contractility by the phospholamban/SERCA2a regulatome.

            Evangelia Kranias, Roger J. Hajjar (2012)
            Heart disease remains the leading cause of death and disability in the Western world. Current therapies aim at treating the symptoms rather than the subcellular mechanisms, underlying the etiology and pathological remodeling in heart failure. A universal characteristic, contributing to the decreased contractile performance in human and experimental failing hearts, is impaired calcium sequestration into the sarcoplasmic reticulum (SR). SR calcium uptake is mediated by a Ca(2+)-ATPase (SERCA2), whose activity is reversibly regulated by phospholamban (PLN). Dephosphorylated PLN is an inhibitor of SERCA and phosphorylation of PLN relieves this inhibition. However, the initial simple view of a PLN/SERCA regulatory complex has been modified by our recent identification of SUMO, S100 and the histidine-rich Ca-binding protein as regulators of SERCA activity. In addition, PLN activity is regulated by 2 phosphoproteins, the inhibitor-1 of protein phosphatase 1 and the small heat shock protein 20, which affect the overall SERCA-mediated Ca-transport. This review will highlight the regulatory mechanisms of cardiac contractility by the multimeric SERCA/PLN-ensemble and the potential for new therapeutic avenues targeting this complex by using small molecules and gene transfer methods.
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              The Structure and Function of the Na,K-ATPase Isoforms in Health and Disease

              Michael Clausen, Florian Hilbers, Hanne Damgaard Poulsen (2017)
              The sodium and potassium gradients across the plasma membrane are used by animal cells for numerous processes, and the range of demands requires that the responsible ion pump, the Na,K-ATPase, can be fine-tuned to the different cellular needs. Therefore, several isoforms are expressed of each of the three subunits that make a Na,K-ATPase, the alpha, beta and FXYD subunits. This review summarizes the various roles and expression patterns of the Na,K-ATPase subunit isoforms and maps the sequence variations to compare the differences structurally. Mutations in the Na,K-ATPase genes encoding alpha subunit isoforms have severe physiological consequences, causing very distinct, often neurological diseases. The differences in the pathophysiological effects of mutations further underline how the kinetic parameters, regulation and proteomic interactions of the Na,K-ATPase isoforms are optimized for the individual cellular needs.
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                Author and article information

                Journal
                Title: Annual Review of Biochemistry
                Abbreviated Title: Annu. Rev. Biochem.
                Publisher: Annual Reviews
                ISSN (Print): 0066-4154
                ISSN (Electronic): 1545-4509
                Publication date Created: June 20 2020
                Publication date (Print): June 20 2020
                Volume: 89
                Issue: 1
                Pages: 583-603
                Affiliations
                [1 ]Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus, Denmark;
                [2 ]Danish Research Institute of Translational Neuroscience (DANDRITE), Nordic European Molecular Biology Laboratory (EMBL) Partnership for Molecular Medicine, 8000 Aarhus, Denmark
                Article
                DOI: 10.1146/annurev-biochem-010611-112801
                PubMed ID: 31874046
                SO-VID: 92ceba0d-ef97-469b-ae28-5317446ef77d
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