ArticleThe Journal of cell biology2010
The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step.
Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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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
34 citing papers in PubMed, 65 citations in OpenAlex.
- Article
- From Pits to Plaques: Electron Microscopy Reveals Clathrin Structural Plasticity in Trafficking, Sorting and Adhesion.Traffic (Copenhagen, Denmark) · 2026Review
- GLUT4 Trafficking and Storage Vesicles: Molecular Architecture, Regulatory Networks, and Their Disruption in Insulin Resistance.International journal of molecular sciences · 2025Review
- CHC22 clathrin recruitment to the early secretory pathway requires two-site interaction with SNX5 and p115.The EMBO journal · 2024Article
- Modulation of Glucose Consumption and Uptake in HepG2 Cells by Aqueous Extracts from the Coelomic Fluid of the EdibleBiology · 2024Article
- Impaired Retrograde Transport Due to Lack of TBC1D5 Contributes to the Trafficking Defect of Lysosomal Cathepsins in Ischemic/Hypoxic Cardiomyocytes.Frontiers in cardiovascular medicine · 2021Article
- Structure, function and regulation of mammalian glucose transporters of the SLC2 family.Pflugers Archiv : European journal of physiology · 2020Review
- CHC22 clathrin mediates traffic from early secretory compartments for human GLUT4 pathway biogenesis.The Journal of cell biology · 2020Article
- GLUT4 Storage Vesicles: Specialized Organelles for Regulated Trafficking.The Yale journal of biology and medicine · 2019Review
- In the line-up: deleted genes associated with DiGeorge/22q11.2 deletion syndrome: are they all suspects?Journal of neurodevelopmental disorders · 2019Review
- Article
- Clathrin heavy chain 22 contributes to the control of neuropeptide degradation and secretion during neuronal development.Scientific reports · 2018Article
- CHC22 and CHC17 clathrins have distinct biochemical properties and display differential regulation and function.The Journal of biological chemistry · 2017Article
- Cell-autonomous adiposity through increased cell surface GLUT4 due to ankyrin-B deficiency.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Sortilin and retromer mediate retrograde transport of Glut4 in 3T3-L1 adipocytes.Molecular biology of the cell · 2017Article
- A novel disorder reveals clathrin heavy chain-22 is essential for human pain and touch development.Brain : a journal of neurology · 2015Article
- Unconventional functions for clathrin, ESCRTs, and other endocytic regulators in the cytoskeleton, cell cycle, nucleus, and beyond: links to human disease.Cold Spring Harbor perspectives in biology · 2014Review
- Clathrin light chains are required for the gyrating-clathrin recycling pathway and thereby promote cell migration.Nature communications · 2014Article
- Actin scaffolding by clathrin heavy chain is required for skeletal muscle sarcomere organization.The Journal of cell biology · 2014Article
- Oleate prevents saturated-fatty-acid-induced ER stress, inflammation and insulin resistance in skeletal muscle cells through an AMPK-dependent mechanism.Diabetologia · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Clathrin heavy chain 22 (CHC22) is an isoform of the well-characterized CHC17 clathrin heavy chain, a coat component of vesicles that mediate endocytosis and organelle biogenesis. CHC22 has a distinct role from CHC17 in trafficking glucose transporter 4 (GLUT4) in skeletal muscle and fat, though its transfection into HEK293 cells suggests functional redundancy. Here, we show that CHC22 is eightfold less abundant than CHC17 in muscle, other cell types have variably lower amounts of CHC22, and endogenous CHC22 and CHC17 function independently in nonmuscle and muscle cells. CHC22 was required for retrograde trafficking of certain cargo molecules from endosomes to the trans-Golgi network (TGN), defining a novel endosomal-sorting step distinguishable from that mediated by CHC17 and retromer. In muscle cells, depletion of syntaxin 10 as well as CHC22 affected GLUT4 targeting, establishing retrograde endosome-TGN transport as critical for GLUT4 trafficking. Like CHC22, syntaxin 10 is not expressed in mice but is present in humans and other vertebrates, implicating two species-restricted endosomal traffic proteins in GLUT4 transport.
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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.