Relative expression of sarco-endoplasmic reticulum calcium ATPase protein in crayfish, Procambarus clarkii, during molting and in response to cold temperature

SciVee ◽  
2008 ◽  
Keyword(s):  
Endoplasmic Reticulum ◽  
Procambarus Clarkii ◽  
Calcium Atpase ◽  
Cold Temperature ◽  
Relative Expression ◽  
Endoplasmic Reticulum Calcium

scholarly journals Cytosolic Phosphorylation of Calnexin Controls Intracellular Ca2+ Oscillations via an Interaction with Serca2b

2000 ◽  
Vol 149 (6) ◽  
pp. 1235-1248 ◽  
Author(s):  
H. Llewelyn Roderick ◽  
James D. Lechleiter ◽  
Patricia Camacho
Keyword(s):  
Endoplasmic Reticulum ◽  
Xenopus Oocytes ◽  
Transmembrane Protein ◽  
Calcium Atpase ◽  
Site Directed Mutagenesis ◽  
Serine Residue ◽  
Endoplasmic Reticulum Calcium ◽  
Inositol 1,4,5 Trisphosphate ◽  
Functional Inhibition ◽  
Cytosolic Domain

Calreticulin (CRT) and calnexin (CLNX) are lectin chaperones that participate in protein folding in the endoplasmic reticulum (ER). CRT is a soluble ER lumenal protein, whereas CLNX is a transmembrane protein with a cytosolic domain that contains two consensus motifs for protein kinase (PK) C/proline- directed kinase (PDK) phosphorylation. Using confocal Ca2+ imaging in Xenopus oocytes, we report here that coexpression of CLNX with sarco endoplasmic reticulum calcium ATPase (SERCA) 2b results in inhibition of intracellular Ca2+ oscillations, suggesting a functional inhibition of the pump. By site-directed mutagenesis, we demonstrate that this interaction is regulated by a COOH-terminal serine residue (S562) in CLNX. Furthermore, inositol 1,4,5-trisphosphate– mediated Ca2+ release results in a dephosphorylation of this residue. We also demonstrate by coimmunoprecipitation that CLNX physically interacts with the COOH terminus of SERCA2b and that after dephosphorylation treatment, this interaction is significantly reduced. Together, our results suggest that CRT is uniquely regulated by ER lumenal conditions, whereas CLNX is, in addition, regulated by the phosphorylation status of its cytosolic domain. The S562 residue in CLNX acts as a molecular switch that regulates the interaction of the chaperone with SERCA2b, thereby affecting Ca2+ signaling and controlling Ca2+-sensitive chaperone functions in the ER.

scholarly journals Survival of Cancer Stem-Like Cells Under Metabolic Stress via CaMK2α-mediated Upregulation of Sarco/Endoplasmic Reticulum Calcium ATPase Expression

2017 ◽  
Vol 24 (7) ◽  
pp. 1677-1690 ◽  
Author(s):  
Ki Cheong Park ◽  
Seung Won Kim ◽  
Jeong Yong Jeon ◽  
A. Ra Jo ◽  
Hye Ji Choi ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Metabolic Stress ◽  
Calcium Atpase ◽  
Endoplasmic Reticulum Calcium

scholarly journals Insulin Receptor Signaling and Sarco/Endoplasmic Reticulum Calcium ATPase in  -Cells

Diabetes ◽  
2002 ◽  
Vol 51 (Supplement 3) ◽  
pp. S427-S433 ◽  
Author(s):  
P. D. Borge ◽  
J. Moibi ◽  
S. R. Greene ◽  
M. Trucco ◽  
R. A. Young ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Insulin Receptor ◽  
Calcium Atpase ◽  
Receptor Signaling ◽  
Endoplasmic Reticulum Calcium ◽  
Insulin Receptor Signaling ◽  
In Cells
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