
Sara Linse
Professor

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