GRAM marks the spot for STIM. Commentary on "GRAM domain proteins specialize functionally distinct ER-PM contact sites in human cells"

Paula Nunes; Nicolas Demaurex

doi:10.1016/j.ceca.2018.04.002

GRAM marks the spot for STIM. Commentary on "GRAM domain proteins specialize functionally distinct ER-PM contact sites in human cells"

Cell Calcium. 2018 Jul:73:70-71. doi: 10.1016/j.ceca.2018.04.002. Epub 2018 Apr 18.

Authors

Paula Nunes¹, Nicolas Demaurex²

Affiliations

¹ Department of Cell Physiology and Metabolism, Rue Michel-Servet, 1, University of Geneva, Switzerland.
² Department of Cell Physiology and Metabolism, Rue Michel-Servet, 1, University of Geneva, Switzerland. Electronic address: Nicolas.Demaurex@unige.ch.

PMID: 29684786
DOI: 10.1016/j.ceca.2018.04.002

Abstract

GRAM domain proteins were reported as novel ER-PM tethers defining specific membrane contact sites (MCS) subdomains. GRAMD2a pre-marks the sites occupied by STIM1 at MCS and its ablation impairs STIM1 translocation, but not store-operated Ca²⁺ entry. We discuss these apparently counterintuitive findings in the context of STIM/ORAI signaling at MCS.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Calcium*
Humans
Neoplasm Proteins
ORAI1 Protein*
Signal Transduction
Stromal Interaction Molecule 1

Substances

Neoplasm Proteins
ORAI1 Protein
Stromal Interaction Molecule 1
Calcium