Regulation of Ca2+ Transport ATPases by Amino- and Carboxy-Terminal Extensions: Mechanisms and (Patho)Physiological Implications

Chen, Jialin; Smaardijk, Susanne; Vandecaetsbeek, Ilse; Vangheluwe, Peter

doi:10.1007/978-3-319-24780-9_14

Cited by 1 publication

(1 citation statement)

References 198 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The discrete properties of the different Ca 2+ -ATPases likely arise from isoform-specific residues that alter the intramolecular network of salt bridges and hydrogen bonds, which may change the molecular dynamics of the pump and affect the rate of conformational transitions (Sitsel et al 2019). Other Ca 2+ -ATPase isoforms, like SERCA2b, SPCA1-2, and PMCA1-4, contain extra protein stretches, mainly at the amino and/or carboxyl terminus, which provide additional regulatory control (Chen et al 2016). Finally, isoformspecific residues participate in regulation by including sites for protein interactions or posttranslational modifications ([PTMs]; Sitsel et al 2019).…”

Section: Conservation and Modulation Of The Ca 2+ Transport Mechanismmentioning

confidence: 99%

Primary Active Ca²⁺ Transport Systems in Health and Disease

Chen

Sitsel

Benoy

et al. 2019

Cold Spring Harb Perspect Biol

Self Cite

View full text Add to dashboard Cite

Calcium ions (Ca 2+ ) are prominent cell signaling effectors that regulate a wide variety of cellular processes. Among the different players in Ca 2+ homeostasis, primary active Ca 2+ transporters are responsible for keeping low basal Ca 2+ levels in the cytosol while establishing steep Ca 2+ gradients across intracellular membranes or the plasma membrane. This review summarizes our current knowledge on the three types of primary active Ca 2+ -ATPases: the sarco(endo)plasmic reticulum Ca 2+ -ATPase (SERCA) pumps, the secretory pathway Ca 2+ -ATPase (SPCA) isoforms, and the plasma membrane Ca 2+ -ATPase (PMCA) Ca 2+ -transporters. We first discuss the Ca 2+ transport mechanism of SERCA1a, which serves as a reference to describe the Ca 2+ transport of other Ca 2+ pumps. We further highlight the common and unique features of each isoform and review their structure-function relationship, expression pattern, regulatory mechanisms, and specific physiological roles. Finally, we discuss the increasing genetic and in vivo evidence that links the dysfunction of specific Ca 2+ -ATPase isoforms to a broad range of human pathologies, and highlight emerging therapeutic strategies that target Ca 2+ pumps.

show abstract

Section: Conservation and Modulation Of The Ca 2+ Transport Mechanismmentioning

confidence: 99%