Title: The Ca2+ Pumps of the Endoplasmic Reticulum and Golgi Apparatus
Authors: Vandecaetsbeek, Ilse ×
Vangheluwe, Peter
Raeymaekers, Luc
Wuytack, Frank
Vanoevelen, Jo #
Issue Date: May-2011
Publisher: Cold Spring Harbor Laboratory Press
Series Title: Cold Spring Harbor Perspectives in Biology vol:3 issue:5 pages:-
Article number: a004184
Abstract: The various splice variants of the three SERCA- and the two SPCA-pump genes in higher vertebrates encode P-type ATPases of the P-2A group found respectively in the membranes of the endoplasmic reticulum and the secretory pathway. Of these, SERCA2b and SPCA1a represent the housekeeping isoforms. The SERCA2b form is characterized by a luminal carboxy terminus imposing a higher affinity for cytosolic Ca2+ compared to the other SERCAs. This is mediated by intramembrane and luminal interactions of this extension with the pump. Other known affinity modulators like phospholamban and sarcolipin decrease the affinity for Ca2+. The number of proteins reported to interact with SERCA is rapidly growing. Here, we limit the discussion to those for which the interaction site with the ATPase is specified: HAX-1, calumenin, histidine-rich Ca2+-binding protein, and indirectly calreticulin, calnexin, and ERp57. The role of the phylogenetically older and structurally simpler SPCAs as transporters of Ca2+, but also of Mn2+, is also addressed.
ISSN: 1943-0264
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Cellular Transport Systems
× corresponding author
# (joint) last author

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