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Portrait of Sara Snogerup Linse

Sara Linse

Professor

Portrait of Sara Snogerup Linse

Calmodulin Binding to the Polybasic C-Termini of STIM Proteins Involved in Store-Operated Calcium Entry.

Author

  • Mikael Bauer
  • David O'Connell
  • Dolores Cahill
  • Sara Linse

Summary, in English

Translocation of STIM1 and STIM2 from the endoplasmic reticulum to the plasma membrane is a key step in store-operated calcium entry in the cell. We show by isothermal titration calorimetry that calmodulin binds in a calcium-dependent manner to the polybasic C-termini of STIM1 and STIM2, a region critical for their translocation to the plasma membrane ( K D </= 1 microM in calcium). HSQC NMR spectroscopy shows this interaction is in the fast exchange regime. By binding STIM1 and STIM2, calmodulin may regulate store refilling, thereby ensuring the maintenance of its own action in intracellular signaling.

Department/s

  • Biophysical Chemistry

Publishing year

2008

Language

English

Pages

6089-6091

Publication/Series

Biochemistry

Volume

47

Issue

23

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Biochemistry and Molecular Biology

Status

Published

ISBN/ISSN/Other

  • ISSN: 0006-2960