ArticleMolecular biology of the cell2011
A variable cytoplasmic domain segment is necessary for γ-protocadherin trafficking and tubulation in the endosome/lysosome pathway.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- 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
- Astrocyte morphogenesis requires self-recognition.Nature · 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
- Visualization ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- A Unique Role for Protocadherin γC3 in Promoting Dendrite Arborization through an Axin1-Dependent Mechanism.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Ubiquitination of the protocadherin-γA3 variable cytoplasmic domain modulates cell-cell interaction.Frontiers in cell and developmental biology · 2023Article
- Trans-splicing facilitated by RNA pairing greatly expands sDscam isoform diversity but not homophilic binding specificity.Science advances · 2022Article
- Identification of a genetic variant underlying familial cases of recurrent benign paroxysmal positional vertigo.PloS one · 2021Article
- The γ-Protocadherins Regulate the Survival of GABAergic Interneurons during Developmental Cell Death.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- 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 clustered protocadherin endolysosomal trafficking motif mediates cytoplasmic association.BMC cell biology · 2015Article
- Protein Kinase C Phosphorylation of a γ-Protocadherin C-terminal Lipid Binding Domain Regulates Focal Adhesion Kinase Inhibition and Dendrite Arborization.The Journal of biological chemistry · 2015Article
- Cadherin-based transsynaptic networks in establishing and modifying neural connectivity.Current topics in developmental biology · 2015Review
- Protocadherins, not prototypical: a complex tale of their interactions, expression, and functions.Frontiers in molecular neuroscience · 2013Article
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6 authors at 1 institution in 1 country.
Funding
Abstract
Clustered protocadherins (Pcdhs) are arranged in gene clusters (α, β, and γ) with variable and constant exons. Variable exons encode cadherin and transmembrane domains and ~90 cytoplasmic residues. The 14 Pcdh-αs and 22 Pcdh-γs are spliced to constant exons, which, for Pcdh-γs, encode ~120 residues of an identical cytoplasmic moiety. Pcdh-γs participate in cell-cell interactions but are prominently intracellular in vivo, and mice with disrupted Pcdh-γ genes exhibit increased neuronal cell death, suggesting nonconventional roles. Most attention in terms of Pcdh-γ intracellular interactions has focused on the constant domain. We show that the variable cytoplasmic domain (VCD) is required for trafficking and organelle tubulation in the endolysosome system. Deletion of the constant cytoplasmic domain preserved the late endosomal/lysosomal trafficking and organelle tubulation observed for the intact molecule, whereas deletion or excision of the VCD or replacement of the Pcdh-γA3 cytoplasmic domain with that from Pcdh-α1 or N-cadherin dramatically altered trafficking. Truncations or internal deletions within the VCD defined a 26-amino acid segment required for trafficking and tubulation in the endolysosomal pathway. This active VCD segment contains residues that are conserved in Pcdh-γA and Pcdh-γB subfamilies. Thus the VCDs of Pcdh-γs mediate interactions critical for Pcdh-γ trafficking.
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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.