Calmodulin Binding to the Polybasic C-Termini of STIM Proteins Involved in Store-Operated Calcium Entry-Reference-Cited by-同舟云学术

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

Published:2008-05-17 Issue:23 Volume:47 Page:6089-6091
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bauer Mikael C.¹,O’Connell David¹,Cahill Dolores J.¹,Linse Sara¹

Affiliation:

1. Lund University, Biophysical Chemistry, Chemical Centre, P O Box 124, SE221 00 Lund, Sweden, and Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800496a

Reference23 articles.

1. STIM Is a Ca2+ Sensor Essential for Ca2+-Store-Depletion-Triggered Ca2+ Influx

2. STIM1, an essential and conserved component of store-operated Ca2+ channel function

3. STIM2 Is a Feedback Regulator that Stabilizes Basal Cytosolic and Endoplasmic Reticulum Ca2+ Levels

4. Identification and characterization of the STIM (stromal interaction molecule) gene family: coding for a novel class of transmembrane proteins

5. STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane

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