Genes of interest, especially multiple-copy genes, is needed before performing gene

Genes of interest, especially multiple-copy genes, is needed before performing gene expression or comparative studies. The availability of many sequenced genomes greatly facilitates the investigation of the evolutionary history of many environmentally relevant gene families, such as the P-type II ATPases. This family of cation transporters plays a key role in the adaptation of organisms to variable environments, including variation in cation concentrations, due to their shared specificities for Ca2+, K+ and Na+ [1]. Although the nomenclature of this gene family has been revisited, it is generally accepted that P-type II ATPases include five closely related sub-families (SERCA, PMCA, NK/HK, ENA, and ACU) [1,2,3]. This study focuses on investigating the key evolutionary events that have led to the extensive diversification of sarco(endo)plasmic calcium ATPases (SERCA) across the major domains of eukaryotes.Scarco(endo)plasmic Reticulum Calcium-ATPase (SERCA) is a key player in calcium signalling [4], which is involved in many aspects of cellular function [5], including transcription [6], cell motility [7], apoptosis, exocytosis, and signal CAL 120 biological activity transduction [8]. For example, during calcium-mediated signal transduction, the depolarization of the cell membrane in active cells causes an extensive influx of calcium into the cytoplasm. However, this influx of calcium needs to be reversed for proper cellular function [5]. To reduce cytoplasmic Ca2+ concentrations, SERCA uses ATP to actively pump calcium into the sarco(endo)plasmic reticulum for storage [4,9]. The essential cellular function of SERCA makes it an interesting Madrasin target for evolutionary studies as it is ubiquitous and indispensable across eukaryotic taxa. Given the importance of the SERCA proteins to both cellular and organismal physiology, changes in the function, location, and expression of SERCA constitute significant evolutionary events. Previous genetic studies revealed that several gene duplication events occurred in the evolution of the SERCA. Three genes are present in vertebrates (ATP2A1-3), coding for three SERCA isoforms, SERCA 1-3 [9], while only one gene has been described in invertebrates, with the exception of the human parasitic blood fluke, Schistosoma mansoni, which has at least two [9,10]. Interestingly, each of the vertebrate genes undergoes alternative splicing, resulting in ten SERCA proteins: SERCA 1a/b, SERCA 2a/b and SERCA 3a/b/c/d/e/f [11,12]. These isoforms andThe Evolution of Sarco(endo)plasmic Calcium ATPasetheir splice variants show a range of tissue specific expression patterns. For example, SERCA 1a is expressed in fast twitch muscles of adults and SERCA 1b in neonates [13]. SERCA 2a is expressed primarily in cardiac and slow-twitch skeletal muscles, whereas its splice variant, SERCA 2b, is expressed in almost all non-muscle cells and is often considered the house keeping variant [9,12]. Furthermore, SERCAs 3 and 2b are found in a wide range of cells including lymphocytes, epithelial, endothelial, and mast cells, as well as Purkinje neurons of the cerebellum [9,14]. The efficiency of the pump varies among the isoforms with SERCA 1a/b having a higher turnover rate than SERCA 2b and a higher affinity for calcium than SERCA 3 [14,15]. Between the two SERCA 2 isoforms, SERCA 2b has a 2-fold higher calcium binding ability but a 2-fold lower turnover rate [14,16]. The single SERCA gene in invertebrates also undergoes alternative splicing and shows tissue specific.Genes of interest, especially multiple-copy genes, is needed before performing gene expression or comparative studies. The availability of many sequenced genomes greatly facilitates the investigation of the evolutionary history of many environmentally relevant gene families, such as the P-type II ATPases. This family of cation transporters plays a key role in the adaptation of organisms to variable environments, including variation in cation concentrations, due to their shared specificities for Ca2+, K+ and Na+ [1]. Although the nomenclature of this gene family has been revisited, it is generally accepted that P-type II ATPases include five closely related sub-families (SERCA, PMCA, NK/HK, ENA, and ACU) [1,2,3]. This study focuses on investigating the key evolutionary events that have led to the extensive diversification of sarco(endo)plasmic calcium ATPases (SERCA) across the major domains of eukaryotes.Scarco(endo)plasmic Reticulum Calcium-ATPase (SERCA) is a key player in calcium signalling [4], which is involved in many aspects of cellular function [5], including transcription [6], cell motility [7], apoptosis, exocytosis, and signal transduction [8]. For example, during calcium-mediated signal transduction, the depolarization of the cell membrane in active cells causes an extensive influx of calcium into the cytoplasm. However, this influx of calcium needs to be reversed for proper cellular function [5]. To reduce cytoplasmic Ca2+ concentrations, SERCA uses ATP to actively pump calcium into the sarco(endo)plasmic reticulum for storage [4,9]. The essential cellular function of SERCA makes it an interesting target for evolutionary studies as it is ubiquitous and indispensable across eukaryotic taxa. Given the importance of the SERCA proteins to both cellular and organismal physiology, changes in the function, location, and expression of SERCA constitute significant evolutionary events. Previous genetic studies revealed that several gene duplication events occurred in the evolution of the SERCA. Three genes are present in vertebrates (ATP2A1-3), coding for three SERCA isoforms, SERCA 1-3 [9], while only one gene has been described in invertebrates, with the exception of the human parasitic blood fluke, Schistosoma mansoni, which has at least two [9,10]. Interestingly, each of the vertebrate genes undergoes alternative splicing, resulting in ten SERCA proteins: SERCA 1a/b, SERCA 2a/b and SERCA 3a/b/c/d/e/f [11,12]. These isoforms andThe Evolution of Sarco(endo)plasmic Calcium ATPasetheir splice variants show a range of tissue specific expression patterns. For example, SERCA 1a is expressed in fast twitch muscles of adults and SERCA 1b in neonates [13]. SERCA 2a is expressed primarily in cardiac and slow-twitch skeletal muscles, whereas its splice variant, SERCA 2b, is expressed in almost all non-muscle cells and is often considered the house keeping variant [9,12]. Furthermore, SERCAs 3 and 2b are found in a wide range of cells including lymphocytes, epithelial, endothelial, and mast cells, as well as Purkinje neurons of the cerebellum [9,14]. The efficiency of the pump varies among the isoforms with SERCA 1a/b having a higher turnover rate than SERCA 2b and a higher affinity for calcium than SERCA 3 [14,15]. Between the two SERCA 2 isoforms, SERCA 2b has a 2-fold higher calcium binding ability but a 2-fold lower turnover rate [14,16]. The single SERCA gene in invertebrates also undergoes alternative splicing and shows tissue specific.

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