ReviewSeminars in cell & developmental biology2009
Signal peptide peptidases: a family of intramembrane-cleaving proteases that cleave type 2 transmembrane proteins.
Review in Seminars in cell & developmental biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
37 citing papers in PubMed, 62 citations in OpenAlex.
- Article
- Activation of the PDGF β Receptor by a Persistent Artificial Signal Peptide.Journal of molecular biology · 2021Article
- Blocking HSV-1 glycoprotein K binding to signal peptide peptidase reduces virus infectivity in vitro and in vivo.PLoS pathogens · 2021Article
- Bioinformatic mapping of a more precise Aspergillus niger degradome.Scientific reports · 2021Article
- Yeast-based reporter assay system for identifying the requirements of intramembrane proteolysis by signal peptide peptidase of Arabidopsis thaliana.FEBS open bio · 2020Article
- Absence of Signal Peptide Peptidase, an Essential Herpes Simplex Virus 1 Glycoprotein K Binding Partner, Reduces Virus InfectivityJournal of virology · 2019Article
- Signal peptide peptidase-like 2c impairs vesicular transport and cleaves SNARE proteins.EMBO reports · 2019Article
- The intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban.EMBO reports · 2019Article
- The potent effect of mycolactone on lipid membranes.PLoS pathogens · 2018Article
- Intramembrane Proteolysis of Astrotactins.The Journal of biological chemistry · 2017Article
- Bunyamwera orthobunyavirus glycoprotein precursor is processed by cellular signal peptidase and signal peptide peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Complex Formed between Intramembrane Metalloprotease SpoIVFB and Its Substrate, Pro-σK.The Journal of biological chemistry · 2016Article
- Differential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase Inhibitors.PloS one · 2015Article
- Dissection of key determinants of cleavage activity in signal peptidase III (SPaseIII) PibD.Extremophiles : life under extreme conditions · 2014Article
- Cleavage by signal peptide peptidase is required for the degradation of selected tail-anchored proteins.The Journal of cell biology · 2014Article
- Genome-wide analysis of regulatory proteases sequences identified through bioinformatics data mining in Taenia solium.BMC genomics · 2014Article
- Inhibitors of signal peptide peptidase (SPP) affect HSV-1 infectivity in vitro and in vivo.Experimental eye research · 2014Article
- The intramembrane proteases signal Peptide peptidase-like 2a and 2b have distinct functions in vivo.Molecular and cellular biology · 2014Article
- Binding of HSV-1 glycoprotein K (gK) to signal peptide peptidase (SPP) is required for virus infectivity.PloS one · 2014Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Five genes encode the five human signal peptide peptidases (SPPs), which are intramembrane-cleaving aspartyl proteases (aspartyl I-CLiPs). SPPs have been conserved through evolution with family members found in higher eukaryotes, fungi, protozoa, arachea, and plants. SPPs are related to the presenilin family of aspartyl I-CLiPs but differ in several key aspects. Presenilins (PSENs) and SPPs both cleave the transmembrane region of membrane proteins; however, PSENs cleave type 1 membrane proteins whereas SPPs cleave type 2 membrane proteins. Though the overall homology between SPPs and PSENs is minimal, they are multipass membrane proteins that contain two conserved active site motifs YD and GxGD in adjacent membrane-spanning domains and a conserved PAL motif of unknown function near their COOH-termini. They differ in that the active site YD and GxGD containing transmembrane domains of SPPs are inverted relative to PSENs, thus, orienting the active site in a consistent topology relative to the substrate. At least two of the human SPPs (SPP and SPPL3) appear to function without additional cofactors, but PSENs function as a protease, called gamma-secretase, only when complexed with Nicastrin, APH-1 and Pen-2. The biological roles of SPP are largely unknown, and only a few endogenous substrates for SPPs have been identified. Nevertheless there is emerging evidence that SPP family members are highly druggable and may regulate both essential physiologic and pathophysiologic processes. Further study of the SPP family is needed in order to understand their biological roles and their potential as therapeutic targets.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.