ArticleThe Journal of biological chemistry2009
p120 catenin recruits cadherins to gamma-secretase and inhibits production of Abeta peptide.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Adherens junctions organize size-selective proteolytic hotspots critical for Notch signalling.Nature cell biology · 2022Article
- Alzheimer's disease amyloid-β pathology in the lens of the eye.Experimental eye research · 2022Article
- Delta-Catenin as a Modulator of Rho GTPases in Neurons.Frontiers in cellular neuroscience · 2022Review
- Recent Advances in Our Understanding of the Infectious Entry Pathway of Human Papillomavirus Type 16.Microorganisms · 2021Review
- Review
- p120 catenin recruits HPV to γ-secretase to promote virus infection.PLoS pathogens · 2020Article
- Article
- Functional roles of p120ctn family of proteins in central neurons.Seminars in cell & developmental biology · 2017Review
- Article
- Epithelial-to-Mesenchymal Plasticity Harnesses Endocytic Circuitries.Frontiers in oncology · 2015Review
- Presenilin-1/γ-secretase controls glutamate release, tyrosine phosphorylation, and surface expression of N-methyl-D-aspartate receptor (NMDAR) subunit GluN2B.The Journal of biological chemistry · 2013Article
- Interactome analyses of mature γ-secretase complexes reveal distinct molecular environments of presenilin (PS) paralogs and preferential binding of signal peptide peptidase to PS2.The Journal of biological chemistry · 2013Article
- Cellular mechanisms of γ-secretase substrate selection, processing and toxicity.Progress in neurobiology · 2012Review
- δ-Catenin promotes E-cadherin processing and activates β-catenin-mediated signaling: implications on human prostate cancer progression.Biochimica et biophysica acta · 2012Article
- Cell adhesion molecules in Alzheimer's disease.Degenerative neurological and neuromuscular disease · 2012Review
- Article
- Inhibitors of γ-secretase stabilize the complex and differentially affect processing of amyloid precursor protein and other substrates.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- Synaptic autoregulation by metalloproteases and γ-secretase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Characterizing the RNA targets and position-dependent splicing regulation by TDP-43.Nature neuroscience · 2011Article
- Amyloid-β production via cleavage of amyloid-β protein precursor is modulated by cell density.Journal of Alzheimer's disease : JAD · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The gamma-secretase complex cleaves many transmembrane proteins, including amyloid precursor protein, EphB and ErbB tyrosine kinase receptors, Notch1 receptors, and adhesion factors. Presenilin 1, the catalytic subunit of gamma-secretase, associates with the cadherin/catenin cell-cell adhesion/communication system and promotes cadherin processing (Georgakopoulos, A., et al. (1999) Mol. Cell 4, 893-902; Marambaud, P., et al. (2002) EMBO J. 21, 1948-1956), but the mechanism by which gamma-secretase and cadherins associate is unclear. Here we report that p120 catenin (p120ctn), a component of the cadherin-catenin complex, recruits gamma-secretase to cadherins, thus stimulating their processing while inhibiting production of Abeta peptide and the amyloid precursor protein intracellular domain. This function of p120ctn depends on both p120ctn-cadherin and p120ctn-presenilin 1 binding, indicating that p120ctn is the central factor that bridges gamma-secretase and cadherin-catenin complexes. Our data show that p120ctn is a unique positive regulator of the gamma-secretase processing of cadherins and a negative regulator of the amyloid precursor protein processing. Furthermore, our data suggest that specific members of the gamma-secretase complex may be used to recruit different substrates and that distinct PS1 sequences are required for processing of APP and cadherins.
Indexed as
Identifiers
What OpenQuestion holds
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.