PMID- 23395841
OWN - NLM
STAT- MEDLINE
DCOM- 20131018
LR  - 20161125
IS  - 1873-3913 (Electronic)
IS  - 0898-6568 (Linking)
VI  - 25
IP  - 5
DP  - 2013 May
TI  - The polybasic lysine-rich domain of plasma membrane-resident STIM1 is essential 
      for the modulation of store-operated divalent cation entry by extracellular 
      calcium.
PG  - 1328-37
LID - S0898-6568(13)00036-3 [pii]
LID - 10.1016/j.cellsig.2013.01.025 [doi]
AB  - STIM1 acts as an endoplasmic reticulum Ca(2+) sensor that communicates the 
      filling state of the intracellular stores to the store-operated channels. In 
      addition, STIM1 is expressed in the plasma membrane, with the Ca(2+) binding 
      EF-hand motif facing the extracellular medium; however, its role sensing 
      extracellular Ca(2+) concentrations in store-operated Ca(2+) entry (SOCE), as 
      well as the underlying mechanism remains unclear. Here we report that divalent 
      cation entry stimulated by thapsigargin (TG) is attenuated by extracellular 
      Ca(2+) in a concentration-dependent manner. Expression of the Ca(2+)-binding 
      defective STIM1(D76A) mutant did not alter the surface expression of STIM1 but 
      abolishes the regulation of divalent cation entry by extracellular Ca(2+). Orai1 
      and TRPC1 have been shown to play a major role in SOCE. Expression of the 
      STIM1(D76A) mutant did not alter Orai1 phosphoserine content. TRPC1 silencing 
      significantly attenuated TG-induced Mn(2+) entry. Expression of the 
      STIM1(K684,685E) mutant impaired the association of plasma membrane STIM1 with 
      TRPC1, as well as the regulation of TG-induced divalent cation entry by 
      extracellular Ca(2+), which suggests that TRPC1 might be involved in the 
      regulation of divalent cation entry by extracellular Ca(2+) mediated by plasma 
      membrane-resident STIM1. Expression of the STIM1(D76A) or STIM1(K684,685E) 
      mutants reduced store-operated divalent cation entry and resulted in loss of 
      dependence on the extracellular Ca(2+) concentration, providing evidence for a 
      functional role of plasma membrane-resident STIM1 in the regulation of 
      store-operated divalent cation entry, which at least involves the EF-hand motif 
      and the C-terminal polybasic lysine-rich domain.
CI  - Copyright (c) 2013 Elsevier Inc. All rights reserved.
FAU - Jardin, Isaac
AU  - Jardin I
AD  - Institute of Biophysics, University of Linz, A-4040 Linz, Austria.
FAU - Dionisio, Natalia
AU  - Dionisio N
FAU - Frischauf, Irene
AU  - Frischauf I
FAU - Berna-Erro, Alejandro
AU  - Berna-Erro A
FAU - Woodard, Geoffrey E
AU  - Woodard GE
FAU - Lopez, Jose J
AU  - Lopez JJ
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 - 20130208
PL  - England
TA  - Cell Signal
JT  - Cellular signalling
JID - 8904683
RN  - 0 (Calcium Channels)
RN  - 0 (Cations, Divalent)
RN  - 0 (Membrane Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (ORAI1 Protein)
RN  - 0 (ORAI1 protein, human)
RN  - 0 (RNA, Small Interfering)
RN  - 0 (STIM1 protein, human)
RN  - 0 (Stromal Interaction Molecule 1)
RN  - 0 (TRPC Cation Channels)
RN  - 0 (transient receptor potential cation channel, subfamily C, member 1)
RN  - 25104-18-1 (Polylysine)
RN  - 67526-95-8 (Thapsigargin)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Substitution
MH  - Calcium/*metabolism
MH  - Calcium Channels/genetics/*metabolism
MH  - Cations, Divalent/*metabolism
MH  - Cell Membrane/metabolism
MH  - Gene Expression/drug effects
MH  - HEK293 Cells
MH  - Humans
MH  - Ion Transport/drug effects
MH  - Membrane Proteins/genetics/*metabolism
MH  - Neoplasm Proteins/genetics/*metabolism
MH  - ORAI1 Protein
MH  - Phosphorylation
MH  - Polylysine/chemistry
MH  - Protein Structure, Tertiary
MH  - RNA Interference
MH  - RNA, Small Interfering/metabolism
MH  - Stromal Interaction Molecule 1
MH  - TRPC Cation Channels/antagonists & inhibitors/genetics/metabolism
MH  - Thapsigargin/pharmacology
EDAT- 2013/02/12 06:00
MHDA- 2013/10/19 06:00
CRDT- 2013/02/12 06:00
PHST- 2012/11/13 00:00 [received]
PHST- 2013/01/09 00:00 [revised]
PHST- 2013/01/23 00:00 [accepted]
PHST- 2013/02/12 06:00 [entrez]
PHST- 2013/02/12 06:00 [pubmed]
PHST- 2013/10/19 06:00 [medline]
AID - S0898-6568(13)00036-3 [pii]
AID - 10.1016/j.cellsig.2013.01.025 [doi]
PST - ppublish
SO  - Cell Signal. 2013 May;25(5):1328-37. doi: 10.1016/j.cellsig.2013.01.025. Epub 
      2013 Feb 8.