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Related Experiment Videos

Complete primary structure of a human plasma membrane Ca2+ pump.

A K Verma1, A G Filoteo, D R Stanford

  • 1Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905.

The Journal of Biological Chemistry
|October 5, 1988
PubMed
Summary

Researchers isolated and sequenced cDNAs for a human plasma membrane calcium pump (Ca2+ pump). The findings reveal distinct isozymes, differing from the erythrocyte Ca2+ pump, with key functional and regulatory domains identified.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Plasma membrane calcium pumps (Ca2+ pumps) are crucial for maintaining cellular calcium homeostasis.
  • Understanding the structure and regulation of these pumps is essential for various physiological processes.
  • Previous studies identified conserved functional regions in ion-transporting ATPases.

Purpose of the Study:

  • To isolate and characterize cDNAs encoding a human plasma membrane Ca2+ pump.
  • To identify functional and regulatory domains within the pump protein.
  • To compare the cloned pump with known Ca2+ pumps, such as the erythrocyte Ca2+ pump.

Main Methods:

  • Isolation and sequencing of cDNAs from a human teratoma library.
  • Bioinformatic analysis of the translated amino acid sequence.

Related Experiment Videos

  • Comparison of the deduced protein sequence with known Ca2+ pump sequences.

    • Main Results:

    • Successfully isolated and sequenced cDNAs coding for a 1,220-amino acid plasma membrane Ca2+ pump (134,683 Da).
    • Identified conserved functional regions characteristic of ion-transporting ATPases.
    • Discovered novel domains, including a calmodulin-binding domain, acidic regions, EF hands, and potential phosphorylation sites, suggesting complex regulation.

    Conclusions:

    • The cloned human plasma membrane Ca2+ pump possesses key functional and regulatory domains, including those involved in calcium binding and calmodulin interaction.
    • The identified isozyme exhibits significant sequence homology but is not identical to the erythrocyte Ca2+ pump, indicating distinct functional roles.
    • The carboxyl-terminal region plays a critical role in pump regulation via calmodulin, proteolysis, and phosphorylation.