scholarly journals Archaeal roots of intramembrane aspartyl protease siblings signal peptide peptidase and presenilin

2020 ◽  
Author(s):  
Priyam Raut ◽  
Jennifer B. Glass ◽  
Raquel L. Lieberman
Keyword(s):  
Signal Peptide ◽  
Aspartyl Protease ◽  
Signal Peptide Peptidase

Author response for "Archaeal roots of intramembrane aspartyl protease siblings signal peptide peptidase and presenilin"

2020 ◽  
Author(s):  
Priyam Raut ◽  
Jennifer B. Glass ◽  
Raquel L. Lieberman
Keyword(s):  
Signal Peptide ◽  
Author Response ◽  
Aspartyl Protease ◽  
Signal Peptide Peptidase

scholarly journals A Protease-Independent Function for SPPL3 in NFAT Activation

2014 ◽  
Vol 35 (2) ◽  
pp. 451-467 ◽  
Author(s):  
Stefanie L. Makowski ◽  
Zhaoquan Wang ◽  
Joel L. Pomerantz
Keyword(s):  
T Cell Receptor ◽  
Signal Peptide ◽  
Intracellular Signaling ◽  
Cell Receptor ◽  
Aspartyl Protease ◽  
Independent Function ◽  
Transmembrane Region ◽  
Signal Peptide Peptidase ◽  
Nfat Activation ◽  
And Function

The signal peptide peptidase (SPP)-related intramembrane aspartyl proteases are a homologous group of polytopic membrane proteins, some of which function in innate or adaptive immunity by cleaving proteins involved in antigen presentation or intracellular signaling. Signal peptide peptidase-like 3 (SPPL3) is a poorly characterized endoplasmic reticulum (ER)-localized member of this family, with no validated cellular substrates. We report here the isolation of SPPL3 in a screen for activators of NFAT, a transcription factor that controls lymphocyte development and function. We find that SPPL3 is required downstream of T cell receptor engagement for maximal Ca2+influx and NFAT activation. Surprisingly, the proteolytic activity of SPPL3 is not required for its role in this pathway. SPPL3 enhances the signal-induced association of stromal interaction molecule 1 (STIM1) and Orai1 and is even required for the full activity of constitutively active STIM1 variants that bind Orai1 independently of ER Ca2+release. SPPL3 associates with STIM1 through at least two independent domains, the transmembrane region and the CRAC activation domain (CAD), and can promote the association of the STIM1 CAD with Orai1. Our results assign a function in lymphocyte signaling to SPPL3 and highlight the emerging importance of nonproteolytic functions for members of the intramembrane aspartyl protease family.

scholarly journals Vigilin interacts with signal peptide peptidase

2012 ◽  
Vol 10 (1) ◽  
pp. 33 ◽  
Author(s):  
Stephen Hsueh-Jeng Lu ◽  
Amy Hye Won Jeon ◽  
Gerold Schmitt-Ulms ◽  
Seema Qamar ◽  
Roger Dodd ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Signal Peptide Peptidase

scholarly journals Cloning and overexpression of a thermostable signal peptide peptidase (SppA) fromThermoplasma volcaniumGSS1 inE. coli

2009 ◽  
Vol 4 (7) ◽  
pp. 1054-1054 ◽  
Author(s):  
Semra Kocabıyık ◽  
Burçak Demirok
Keyword(s):  
Signal Peptide ◽  
Signal Peptide Peptidase
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