PMID- 16966422
OWN - NLM
STAT- MEDLINE
DCOM- 20061101
LR  - 20220225
IS  - 0021-9525 (Print)
IS  - 1540-8140 (Electronic)
IS  - 0021-9525 (Linking)
VI  - 174
IP  - 6
DP  - 2006 Sep 11
TI  - Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated 
      with the plasma membrane.
PG  - 803-13
AB  - Stromal interacting molecule 1 (STIM1), reported to be an endoplasmic reticulum 
      (ER) Ca(2+) sensor controlling store-operated Ca(2+) entry, redistributes from a 
      diffuse ER localization into puncta at the cell periphery after store depletion. 
      STIM1 redistribution is proposed to be necessary for Ca(2+) release-activated 
      Ca(2+) (CRAC) channel activation, but it is unclear whether redistribution is 
      rapid enough to play a causal role. Furthermore, the location of STIM1 puncta is 
      uncertain, with recent reports supporting retention in the ER as well as 
      insertion into the plasma membrane (PM). Using total internal reflection 
      fluorescence (TIRF) microscopy and patch-clamp recording from single Jurkat 
      cells, we show that STIM1 puncta form several seconds before CRAC channels open, 
      supporting a causal role in channel activation. Fluorescence quenching and 
      electron microscopy analysis reveal that puncta correspond to STIM1 accumulation 
      in discrete subregions of junctional ER located 10-25 nm from the PM, without 
      detectable insertion of STIM1 into the PM. Roughly one third of these ER-PM 
      contacts form in response to store depletion. These studies identify an ER 
      structure underlying store-operated Ca(2+) entry, whose extreme proximity to the 
      PM may enable STIM1 to interact with CRAC channels or associated proteins.
FAU - Wu, Minnie M
AU  - Wu MM
AD  - Department of Molecular and Cellular Physiology, Stanford University School of 
      Medicine, Stanford, CA 94305, USA.
FAU - Buchanan, JoAnn
AU  - Buchanan J
FAU - Luik, Riina M
AU  - Luik RM
FAU - Lewis, Richard S
AU  - Lewis RS
LA  - eng
GR  - T32 AI007290/AI/NIAID NIH HHS/United States
GR  - GM007276/GM/NIGMS NIH HHS/United States
GR  - T32 GM007276/GM/NIGMS NIH HHS/United States
GR  - R01 GM045374/GM/NIGMS NIH HHS/United States
GR  - R37 GM045374/GM/NIGMS NIH HHS/United States
GR  - 5T32AI07290-21/AI/NIAID NIH HHS/United States
GR  - GM45374/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Calcium Channels)
RN  - 0 (Membrane Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (STIM1 protein, human)
RN  - 0 (Stromal Interaction Molecule 1)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Calcium/*metabolism
MH  - Calcium Channels/*metabolism
MH  - Calcium Signaling/*physiology
MH  - Cell Membrane/*metabolism/ultrastructure
MH  - Cytoplasmic Granules/metabolism/ultrastructure
MH  - Endoplasmic Reticulum/*metabolism/ultrastructure
MH  - Humans
MH  - Intracellular Membranes/metabolism/ultrastructure
MH  - Jurkat Cells
MH  - Membrane Proteins/*metabolism
MH  - Microscopy, Electron
MH  - Microscopy, Fluorescence
MH  - Neoplasm Proteins/*metabolism
MH  - Patch-Clamp Techniques
MH  - Stromal Interaction Molecule 1
PMC - PMC2064335
EDAT- 2006/09/13 09:00
MHDA- 2006/11/02 09:00
PMCR- 2007/03/11
CRDT- 2006/09/13 09:00
PHST- 2006/09/13 09:00 [pubmed]
PHST- 2006/11/02 09:00 [medline]
PHST- 2006/09/13 09:00 [entrez]
PHST- 2007/03/11 00:00 [pmc-release]
AID - jcb.200604014 [pii]
AID - 200604014 [pii]
AID - 10.1083/jcb.200604014 [doi]
PST - ppublish
SO  - J Cell Biol. 2006 Sep 11;174(6):803-13. doi: 10.1083/jcb.200604014.