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SPPL2A signal peptide peptidase-like 2A

PSL2, SPPL2a, intramembrane cleaving protease
This gene encodes a member of the GXGD family of aspartic proteases, which are transmembrane proteins with two conserved catalytic motifs localized within the membrane-spanning regions, as well as a member of the signal peptide peptidase-like protease (SPPL) family. This protein is expressed in all major adult human tissues and localizes to late endosomal compartments and lysosomal membranes. A pseudogene of this gene also lies on chromosome 15. [provided by RefSeq, Feb 2012] (from NCBI)
Top mentioned proteins: CAN, ACID, IgM, Presenilin-1, FBD
Papers on PSL2
Proteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving Proteases.
Haass et al., München, Germany. In J Biol Chem, Feb 2016
The type 2-oriented membrane-retained stub of NRG1 type III is further processed by signal peptide peptidase-like proteases SPPL2a and SPPL2b.
Processing of CD74 by the Intramembrane Protease SPPL2a Is Critical for B Cell Receptor Signaling in Transitional B Cells.
Schröder et al., Kiel, Germany. In J Immunol, Sep 2015
In mice, SPPL2a deficiency provokes the accumulation of this NTF in endocytic vesicles, which leads to a B cell maturation arrest at the transitional 1 stage.
A Cell-Based Assay Reveals Nuclear Translocation of Intracellular Domains Released by SPPL Proteases.
Schröder et al., Kiel, Germany. In Traffic, Aug 2015
During regulated intramembrane proteolysis (RIP) a membrane-spanning substrate protein is cleaved by an ectodomain sheddase and an intramembrane cleaving protease.
Differential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase Inhibitors.
Golde et al., Philadelphia, United States. In Plos One, 2014
The signal peptide peptidases (SPPs) are biomedically important proteases implicated as therapeutic targets for hepatitis C (human SPP, (hSPP)), plasmodium (Plasmodium SPP (pSPP)), and B-cell immunomodulation and neoplasia (signal peptide peptidase like 2a, (SPPL2a)).
Signal-peptide-peptidase-like 2a is required for CD74 intramembrane proteolysis in human B cells.
Schröder et al., Kiel, Germany. In Biochem Biophys Res Commun, 2014
We demonstrated recently that intramembrane proteolysis of the final membrane-bound N-terminal fragment (NTF) of CD74 is catalyzed by Signal-peptide-peptidase-like 2a (SPPL2a) and that this process is indispensable for development and function of B lymphocytes in mice.
Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a).
Hu et al., Ithaca, United States. In J Biol Chem, 2014
The GxGD aspartyl proteases SPPL2a and, to a lesser extent, SPPL2b are responsible for this intramembrane cleavage event.
The intramembrane proteases signal Peptide peptidase-like 2a and 2b have distinct functions in vivo.
Schröder et al., Kiel, Germany. In Mol Cell Biol, 2014
We reported recently that the presenilin homologue signal peptide peptidase-like 2a (SPPL2a) is essential for B cell development by cleaving the N-terminal fragment (NTF) of the invariant chain (li, CD74).
Differential protein-protein interactions of full length human FasL and FasL fragments generated by proteolysis.
Janssen et al., Kiel, Germany. In Exp Cell Res, 2014
These NTFs are further processed by intramembrane proteolysis through signal peptide peptidase-like 2a (SPPL2a), releasing intracellular domains (ICDs) which might translocate to the nucleus to regulate transcription.
γ-Secretase inhibitors and modulators.
Miele et al., Gainesville, United States. In Biochim Biophys Acta, 2013
γ-Secretase is a fascinating, multi-subunit, intramembrane cleaving protease that is now being considered as a therapeutic target for a number of diseases.
Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases.
Fluhrer et al., München, Germany. In Biochim Biophys Acta, 2013
Signal peptide peptidase (SPP) and the homologous SPP-like (SPPL) proteases SPPL2a, SPPL2b, SPPL2c and SPPL3 belong to the family of GxGD intramembrane proteases.
New role of signal peptide peptidase to liberate C-terminal peptides for MHC class I presentation.
van Hall et al., Leiden, Netherlands. In J Immunol, 2013
Moreover, silencing of SPP and its family member SPPL2a led to a general reduction of surface peptide-MHC-I complexes, underlining the involvement of these enzymes in Ag processing and presentation.
The intramembrane protease SPPL2A is critical for tooth enamel formation.
Schröder et al., Amsterdam, Netherlands. In J Bone Miner Res, 2013
Signal-peptide-peptidase-like 2a (SPPL2A), a presenilin-homologue residing in lysosomes/late endosomes, cleaves type II-oriented transmembrane proteins.
Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail.
Schröder et al., Kiel, Germany. In Febs Lett, 2011
Data show that endogenous SPPL2a - in agreement with overexpression studies - is localised in membranes of lysosomes/late endosomes.
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b.
Haass et al., München, Germany. In J Biol Chem, 2008
SPPL2a and SPPL2b mediate the intramembrane cleavage, whereas neither SPP nor SPPL3 is capable of processing the Bri2 N-terminal fragment.
The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells.
Zörnig et al., Frankfurt am Main, Germany. In Cell Death Differ, 2007
ADAM10 and SPPL2a were identified as two proteases implicated in FasL processing and release of the FasL intracellular domain, which has been shown to be important for retrograde FasL signaling
SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production.
Martoglio et al., Zürich, Switzerland. In Nat Cell Biol, 2006
We demonstrate that SPPL2a and SPPL2b, which are sorted to endosomes and the plasma membrane, respectively, are functional proteases that catalyse intramembrane cleavage of tumour necrosis factor alpha (TNFalpha).
(Make) stick and cut loose--disintegrin metalloproteases in development and disease.
Hartmann et al., Leuven, Belgium. In Birth Defects Res C Embryo Today, 2006
A common denominator of ADAM-mediated proteolysis is the ectodomain shedding of a broad spectrum of substrates, including paracrine growth factors like epidermal growth factor receptor (EGFR) ligands, cell adhesion molecules like CD44 or cadherins, and the initiation of regulated intramembrane proteolysis (RIP), whereby the transmembrane fragment of the respective substrate is further cleaved by an intramembrane cleaving protease to release an intracellular domain acting as a nuclear transcription regulator.
Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins.
Martoglio et al., Zürich, Switzerland. In J Biol Chem, 2005
SPP, SPPL2a, -2b, -2c, and -3 probably cleave type II-oriented substrate peptides as shown by consensus analysis
The pea lectin gene family contains only one functional gene.
Strosberg et al., Paris, France. In Plant Mol Biol, 1987
Four positive recombinant phages, λI 101, λI 52, λIII 51 and λIV 22, were isolated and the DNA sequences of the subclones, designated respectively PSL1, PSL2, PSL3 and PSL4, were determined.
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