Modulation of SERCA2 activity: Regulated splicing and interaction with phospholamban

Verboomen, Hilde; Mertens, Luc; Eggermont, Jan; Wuytack, Frank; Bosch, Ludo Van Den

doi:10.1007/bf01788363

Cited by 10 publications

(4 citation statements)

References 47 publications

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“…Modulation of SERCAs adds a further layer of complexity to the different properties of the various of calcium pump isoforms. Phospholamban, which plays a pivota l role in mediating the effects of b-adrenergic stimulation in cardiac muscle, has been the subject of a number of excellent reviews in recent years (Verboomen et al 1995, Simmerman and Jones 1998, Tada and Toyofuku 1998) and, for comprehensiv e coverage of the topic, the reader should consult these articles. Here, only the most recent and major aspects of phospholamban/ SERCA2 interactions will be examined.…”

Section: Modulation Of Serca Activitymentioning

confidence: 99%

Sarco(endo)plasmic reticulum calcium pumps: recent advances in our understanding of structure/function and biology (Review)

2000

Molecular Membrane Biology

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This review examines the structure and function of the sarco(endo)plasmic reticulum calcium pump (SERCA1a) in the light of the recent publication of the 2.6 A resolution structure of this protein, and looks at the increasing awareness of the key role played by SERCAs in calcium signalling. The roles played by the calcium pump isoforms, SERCA1a/b, SERCA2a/b and SERCA3a/b/c in cellular function are discussed, and the modulation of SERCA activity by phospholamban, sarcolipin and other modulatory influences is examined. The recent discoveries of human SERCA mutations leading to disease states is reviewed, and the insights into SERCA function using transgenic approaches are outlined.

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Section: Modulation Of Serca Activitymentioning

confidence: 99%

Sarco(endo)plasmic reticulum calcium pumps: recent advances in our understanding of structure/function and biology (Review)

2000

Molecular Membrane Biology

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“…The SERCA2 gene (ATP2A2) also produces at least two isoforms that are tissue specific. SERCA2a is the principal form of the Ca 2+ -ATPase in adult slow-twitch skeletal and cardiac muscles and in neonatal skeletal muscles (Barndl et al, 1986;MacLennan et al, 1987;Lytton et al, 1988;Wu et al, 1995;Verboomen et al, 1995). It is also expressed at much lower levels in nonmuscle cells (Wu et al, 1995).…”

Section: Classification Of Ca 2+ -Atpase Isoenzymesmentioning

confidence: 99%

The structure of the Ca2+-ATPase of sarcoplasmic reticulum.

Martonosi

Pikula²

2003

Acta Biochim Pol

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In this article the morphology of sarcoplasmic reticulum, classification of Ca(2+)-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology will be reviewed. The focus is on the structure and interactions of Ca(2+)-ATPase determined by electron and X-ray crystallography, lamellar X-ray and neutron diffraction analysis of the profile structure of Ca(2+)-ATPase in sarcoplasmic reticulum multilayers. In addition, targeting of the Ca(2+)-ATPase to the sarcoplasmic reticulum is discussed.

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“…This was achieved by either cloning or labelling the PCR fragments with [α-$#P]dCTP as described previously [5,28]). …”

Section: Cell Culture Dna Transfections Rna Isolation and Reverse Tmentioning

confidence: 99%

Sequence elements surrounding the acceptor site suppress alternative splicing of the sarco/endoplasmic reticulum Ca2+-ATPase 2 gene transcript

Bosch

Mertens

Gijsbers

et al. 1997

Biochemical Journal

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Expression of the muscle-specific 2a isoform of the sarco\ endoplasmic reticulum Ca# + -ATPase (SERCA2) requires activation of an inefficient optional splice process at the 3h end of the primary gene transcript. The sequence elements required for this regulated splice event were studied by modifying a minigene containing the 3h end of the SERCA2 gene. An important requirement appears to be a strong muscle-specific acceptor site, as replacing it by a weak one prevented the induction of muscletype splicing during myogenic differentiation. The induction of muscle-type splicing did not depend on positive cis-active sequences in the muscle-specific exon. On the other hand,

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Modulation of SERCA2 activity: Regulated splicing and interaction with phospholamban

Cited by 10 publications

References 47 publications

Sarco(endo)plasmic reticulum calcium pumps: recent advances in our understanding of structure/function and biology (Review)

Sarco(endo)plasmic reticulum calcium pumps: recent advances in our understanding of structure/function and biology (Review)

The structure of the Ca2+-ATPase of sarcoplasmic reticulum.

Sequence elements surrounding the acceptor site suppress alternative splicing of the sarco/endoplasmic reticulum Ca2+-ATPase 2 gene transcript

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