Literature DB >> 8825033

Modulation of SERCA2 activity: regulated splicing and interaction with phospholamban.

H Verboomen1, L Mertens, J Eggermont, F Wuytack, L Van Den Bosch.   

Abstract

Ca(2+)-uptake into intracellular stores is mediated by the sarco/endoplasmic reticulum Ca(2+)ATPases (SERCAs). This review deals first with the gene structural and the characterization of the tissue-specific SERCA2 transcript processing. Secondly, the two different protein isoforms and their regulation are described. Finally, this review ends with a discussion on the possible physiological role of the SERCA2 isoform diversity.

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Year:  1995        PMID： 8825033     DOI： 10.1007/bf01788363

Source DB:  PubMed          Journal:  Biosci Rep        ISSN： 0144-8463            Impact factor:   3.840


  3 in total

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

Authors:  L Van Den Bosch; L Mertens; S Gijsbers; M V Heyen; F Wuytack; J Eggermont
Journal:  Biochem J       Date:  1997-03-15       Impact factor: 3.857

2.  Alternative processing of the sarco/endoplasmic reticulum Ca(2+)-ATPase transcripts during muscle differentiation is a specifically regulated process.

Authors:  L Van den Bosch; L Mertens; Y Cavaloc; M Peterson; F Wuytack; J Eggermont
Journal:  Biochem J       Date:  1996-08-01       Impact factor: 3.857

Review 3.  Endoplasmic Reticulum-Plasma Membrane Contact Sites as an Organizing Principle for Compartmentalized Calcium and cAMP Signaling.

Authors:  Tim Crul; József Maléth
Journal:  Int J Mol Sci       Date:  2021-04-29       Impact factor: 5.923
  3 in total

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