ArticleJournal of cell science2015
The clathrin-binding and J-domains of GAK support the uncoating and chaperoning of clathrin by Hsc70 in the brain.
Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
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.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Synaptic Proteostasis in Health and Disease.Journal of neurochemistry · 2026Review
- GAK antagonises ROCK-dependent regulation of actomyosin dynamics.Journal of cell science · 2026Article
- Heat shock proteins at the crossroads of endosomal trafficking pathways.Cell biology and toxicology · 2025Review
- Low-frequency genetic variants in GAK enhance Golgi function and protect against Parkinson's disease.medRxiv : the preprint server for health sciences · 2025Article
- Dynamic early recruitment of GAK-Hsc70 regulates coated pit maturation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Podocyte Endocytosis in Regulating the Glomerular Filtration Barrier.Frontiers in medicine · 2022Review
- GAK and PRKCD are positive regulators of PRKN-independent mitophagy.Nature communications · 2021Article
- Dysfunction of Synaptic Vesicle Endocytosis in Parkinson's Disease.Frontiers in integrative neuroscience · 2021Review
- Inhibiting calpain 1 and 2 in cyclin G associated kinase-knockout mice mitigates podocyte injury.JCI insight · 2020Article
- Dynamics of Auxilin 1 and GAK in clathrin-mediated traffic.The Journal of cell biology · 2020Article
- Clathrin heavy chain phosphorylated at T606 plays a role in proper cell division.Cell cycle (Georgetown, Tex.) · 2019Article
- DjA1 maintains Golgi integrity via interaction with GRASP65.Molecular biology of the cell · 2019Article
- Synaptic, Mitochondrial, and Lysosomal Dysfunction in Parkinson's Disease.Trends in neurosciences · 2019Review
- Chemical genetic identification of GAK substrates reveals its role in regulating NaLife science alliance · 2018Article
- Differential regulation of synaptic AP-2/clathrin vesicle uncoating in synaptic plasticity.Scientific reports · 2017Article
- GAK is phosphorylated by c-Src and translocated from the centrosome to chromatin at the end of telophase.Cell cycle (Georgetown, Tex.) · 2017Article
- The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.Frontiers in neuroscience · 2017Review
- Deregulated expression of the HSP40 family members Auxilin-1 and -2 is indicative of proteostasis imbalance and predicts patient outcome in Ph(+) leukemia.Experimental hematology & oncology · 2015Article
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 2 institutions in 1 country.
Funding
Abstract
Cyclin-G-associated kinase (GAK), the ubiquitously expressed J-domain protein, is essential for the chaperoning and uncoating of clathrin that is mediated by Hsc70 (also known as HSPA8). Adjacent to the C-terminal J-domain that binds to Hsc70, GAK has a clathrin-binding domain that is linked to an N-terminal kinase domain through a PTEN-like domain. Knocking out GAK in fibroblasts caused inhibition of clathrin-dependent trafficking, which was rescued by expressing a 62-kDa fragment of GAK, comprising just the clathrin-binding and J-domains. Expressing this fragment as a transgene in mice rescued the lethality and the histological defects caused by knocking out GAK in the liver or in the brain. Furthermore, when both GAK and auxilin (also known as DNAJC6), the neuronal-specific homolog of GAK, were knocked out in the brain, mice expressing the 62-kDa GAK fragment were viable, lived a normal life-span and had no major behavior abnormalities. However, these mice were about half the size of wild-type mice. Therefore, the PTEN-like domains of GAK and auxilin are not essential for Hsc70-dependent chaperoning and uncoating of clathrin, but depending on the tissue, these domains appear to increase the efficiency of these co-chaperones.
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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.