ArticleThe Journal of biological chemistry2010
LC3-dependent intracellular membrane tubules induced by gamma-protocadherins A3 and B2: a role for intraluminal interactions.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 3 of them syntheses that pooled it.
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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.
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Who cites it
31 citing papers in PubMed, 3 syntheses or guidelines pooled it, 41 citations in OpenAlex.
- Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)Autophagy · 2021Guideline
- Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).Autophagy · 2016Guideline
- Guideline
- Reduced Neuronal Self-Avoidance in Mouse Starburst Amacrine Cells With Only One Pcdhg Isoform.Developmental neurobiology · 2026Article
- R406 and its structural analogs reduce SNCA/α-synuclein levels via autophagic degradation.Autophagy · 2025Article
- Surface delivery quantification reveals distinct trafficking efficiencies among clustered protocadherin isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural insights into the in situ assembly of clustered protocadherin γB4.Nature communications · 2025Article
- A C-terminal motif containing a PKC phosphorylation site regulates γ-Protocadherin-mediated dendrite arborization in the cerebral cortex in vivo.Developmental neurobiology · 2024Article
- To eat or not to eat: a critical review on the role of autophagy in prostate carcinogenesis and prostate cancer therapeutics.Frontiers in pharmacology · 2024Review
- Visualization ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Ubiquitination of the protocadherin-γA3 variable cytoplasmic domain modulates cell-cell interaction.Frontiers in cell and developmental biology · 2023Article
- Vault RNAs: hidden gems in RNA and protein regulation.Cellular and molecular life sciences : CMLS · 2021Review
- 'High vault-age': non-coding RNA control of autophagy.Open biology · 2020Review
- Clustered Protocadherins Emerge as Novel Susceptibility Loci for Mental Disorders.Frontiers in neuroscience · 2020Review
- Protocadherins at the Crossroad of Signaling Pathways.Frontiers in molecular neuroscience · 2020Review
- The kinase PERK and the transcription factor ATF4 play distinct and essential roles in autophagy resulting from tunicamycin-induced ER stress.The Journal of biological chemistry · 2019Article
- Sensing Membrane Curvature in Macroautophagy.Journal of molecular biology · 2017Review
- Functional test of PCDHB11, the most human-specific neuronal surface protein.BMC evolutionary biology · 2016Article
- Article
- The clustered protocadherin endolysosomal trafficking motif mediates cytoplasmic association.BMC cell biology · 2015Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Clustered protocadherins (Pcdhs) are a family of cadherin-like molecules arranged in gene clusters (alpha, beta, and gamma). gamma-Protocadherins (Pcdh-gammas) are involved in cell-cell interactions, but their prominent intracellular distribution in vivo and different knock-out phenotypes suggest that these molecules participate in still unidentified processes. We found using correlative light and electron microscopy that Pcdh-gammaA3 and -gammaB2, but not -gammaC4, -alpha1, or N-cadherin, generate intracellular juxtanuclear membrane tubules when expressed in cells. These tubules recruit the autophagy marker MAP1A/1B LC3 (LC3) but are not associated with autophagic vesicles. Lipidation of LC3 is required for its coclustering with Pcdh-gamma tubules, suggesting the involvement of an autophagic-like molecular cascade. Expression of wild-type LC3 with Pcdh-gammaA3 increased tubule length whereas expression of lipidation-defective LC3 decreased tubule length relative to Pcdh-gammaA3 expressed alone. The tubules were found to emanate from lysosomes. Deletion of the luminal/extracellular domain of Pcdh-gammaA3 preserved lysosomal targeting but eliminated tubule formation whereas cytoplasmic deletion eliminated both lysosomal targeting and tubule formation. Deletion of the membrane-proximal three cadherin repeats resulted in tubes that were narrower than those produced by full-length molecules. These results suggest that Pcdh-gammaA and -gammaB families can influence the shape of intracellular membranes by mediating intraluminal interactions within organelles.
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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.