ArticleThe Journal of biological chemistry2015
Presenilin-like GxGD membrane proteases have dual roles as proteolytic enzymes and ion channels.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- Comparative population genomic analyses of transporters within the Asgard archaeal superphylum.PloS one · 2021Article
- Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- PSEN1 Mutant iPSC-Derived Model Reveals Severe Astrocyte Pathology in Alzheimer's Disease.Stem cell reports · 2017Article
- Knockdown of amyloid precursor protein increases calcium levels in the endoplasmic reticulum.Scientific reports · 2017Article
- Dysregulation of neuronal calcium homeostasis in Alzheimer's disease - A therapeutic opportunity?Biochemical and biophysical research communications · 2017Review
- Presenilin adopts the ClC channel fold.Protein science : a publication of the Protein Society · 2016Article
- Approaches to Investigating Complex Genetic Traits in a Large-Scale Inbred Mouse Aging Study.Veterinary pathology · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The GxGD proteases function to cleave protein substrates within the membrane. As these proteases contain multiple transmembrane domains typical of ion channels, we examined if GxGD proteases also function as ion channels. We tested the putative dual function by examining two archeobacterial GxGD proteases (PSH and FlaK), with known three-dimensional structures. Both are in the same GxGD family as presenilin, a protein mutated in Alzheimer Disease. Here, we demonstrate that PSH and FlaK form cation channels in lipid bilayers. A mutation that affected the enzymatic activity of FlaK rendered the channel catalytically inactive and altered the ion selectivity, indicating that the ion channel and the catalytic activities are linked. We report that the GxGD proteases, PSH and FlaK, are true "chanzymes" with interdependent ion channel and protease activity conferred by a single structural domain embedded in the membrane, supporting the proposal that higher-order proteases, including presenilin, have channel function.
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