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

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

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.

Detaljer

Författare
  • Mikael Bauer
  • David O'Connell
  • Dolores Cahill
  • Sara Linse
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biokemi och molekylärbiologi
Originalspråkengelska
Sidor (från-till)6089-6091
TidskriftBiochemistry
Volym47
Utgivningsnummer23
StatusPublished - 2008
PublikationskategoriForskning
Peer review utfördJa