PMID- 21255618
OWN - NLM
STAT- MEDLINE
DCOM- 20110418
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1813
IP  - 3
DP  - 2011 Mar
TI  - Lipid rafts are essential for the regulation of SOCE by plasma membrane resident 
      STIM1 in human platelets.
PG  - 431-7
LID - 10.1016/j.bbamcr.2011.01.010 [doi]
AB  - STIM1 is a transmembrane protein essential for the activation of store-operated 
      Ca(2)+ entry (SOCE), a major Ca(2)+ influx mechanism. STIM1 is either located in the 
      endoplasmic reticulum, communicating the Ca(2)+ concentration in the stores to 
      plasma membrane channels or in the plasma membrane, where it might sense the 
      extracellular Ca(2)+ concentration. Plasma membrane-located STIM1 has been reported 
      to mediate the SOCE sensitivity to extracellular Ca(2)+ through its interaction 
      with Orai1. Here we show that plasma membrane lipid raft domains are essential 
      for the regulation of SOCE by extracellular Ca(2)+. Treatment of platelets with the 
      SERCA inhibitor thapsigargin (TG) induced Mn(2)+ entry, which was inhibited by 
      increasing concentrations of extracellular Ca(2)+. Platelet treatment with 
      methyl-beta-cyclodextrin, which removes cholesterol and disrupts the lipid raft 
      domains, impaired the inactivation of Ca(2)+ entry induced by extracellular Ca(2)+. 
      Methyl-beta-cyclodextrin also abolished translocation of STIM1 to the plasma 
      membrane stimulated by treatment with TG and prevented TG-evoked 
      co-immunoprecipitation between plasma membrane-located STIM1 and the Ca(2)+ 
      permeable channel Orai1. These findings suggest that lipid raft domains are 
      essential for the inactivation of SOCE by extracellular Ca(2)+ mediated by the 
      interaction between plasma membrane-located STIM1 and Orai1.
CI  - Copyright (c) 2011 Elsevier B.V. All rights reserved.
FAU - Dionisio, Natalia
AU  - Dionisio N
AD  - Department of Physiology, Cell Physiology Research Group, University of 
      Extremadura, Caceres, Spain.
FAU - Galan, Carmen
AU  - Galan C
FAU - Jardin, Isaac
AU  - Jardin I
FAU - Salido, Gines M
AU  - Salido GM
FAU - Rosado, Juan A
AU  - Rosado JA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110119
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Calcium Channels)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Membrane Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (ORAI1 Protein)
RN  - 0 (ORAI1 protein, human)
RN  - 0 (STIM1 protein, human)
RN  - 0 (Stromal Interaction Molecule 1)
RN  - 0 (beta-Cyclodextrins)
RN  - 0 (methyl-beta-cyclodextrin)
RN  - 42Z2K6ZL8P (Manganese)
RN  - 67526-95-8 (Thapsigargin)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Blood Platelets/*metabolism
MH  - Calcium/*metabolism
MH  - Calcium Channels/metabolism
MH  - Enzyme Inhibitors/pharmacology
MH  - Humans
MH  - Manganese/metabolism
MH  - Membrane Microdomains/*metabolism
MH  - Membrane Proteins/*metabolism
MH  - Neoplasm Proteins/*metabolism
MH  - ORAI1 Protein
MH  - Stromal Interaction Molecule 1
MH  - Thapsigargin/pharmacology
MH  - beta-Cyclodextrins/metabolism
EDAT- 2011/01/25 06:00
MHDA- 2011/04/19 06:00
CRDT- 2011/01/25 06:00
PHST- 2010/10/13 00:00 [received]
PHST- 2010/12/26 00:00 [revised]
PHST- 2011/01/10 00:00 [accepted]
PHST- 2011/01/25 06:00 [entrez]
PHST- 2011/01/25 06:00 [pubmed]
PHST- 2011/04/19 06:00 [medline]
AID - S0167-4889(11)00018-8 [pii]
AID - 10.1016/j.bbamcr.2011.01.010 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2011 Mar;1813(3):431-7. doi: 10.1016/j.bbamcr.2011.01.010. 
      Epub 2011 Jan 19.