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Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras

DANILO GUERINI^*, FABRIZIO GUIDI and ERNESTO CARAFOLI¹

Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), 8092 Zurich, Switzerland;
^* Novartis Pharma AG, 4002 Basle, Switzerland; and
Department of Biochemistry and Venetian Institute of Molecular Medicine, University of Padova, 35121 Padova, Italy

¹Correspondence: Department of Biochemistry, University of Padova, Viale G. Colombo, 3, 35121 Padova, Italy. E-mail: carafoli{at}civ.bio.unipd.it

Structural features underlying retention of the SERCA pump in intracellular compartments and the sorting of the PMCA pump to the plasma membrane are not known. The biochemical properties of the two pumps suggest that their differential localization may respond to specific functional demands. The two pumps may control Ca²⁺ gradients of different magnitude and dynamic properties. For instance, it has recently become clear that the Ca²⁺ gradient across the endoplasmic reticulum (ER) membrane is smaller than that across the plasma membrane. Previous experiments with chimerical constructs of the SERCA and PMCA pumps had suggested a role for the amino-terminal domain in the ER retention of the SERCA pump. Experiments aimed at narrowing down the region responsible for the retention now indicate that the first 28 amino acids of the SERCA pump may play a role in membrane localization. Results also suggest that the formation of oligomers (possibly through the first 28 amino acids) might be critical to the retention mechanism.—Guerini, D., Guidi, F., Carafoli, E. Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras.

Key Words: plasma membrane Ca²⁺ pump • chimeric proteins • ER/SR Ca²⁺ pump

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