ArticleMolecular biology of the cell2006
Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Dynamic early recruitment of GAK-Hsc70 regulates coated pit maturation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Volleying plasma membrane proteins from birth to death: Role of J-domain proteins.Frontiers in molecular biosciences · 2022Review
- Auxilin-like protein MoSwa2 promotes effector secretion and virulence as a clathrin uncoating factor in the rice blast fungus Magnaporthe oryzae.The New phytologist · 2021Article
- Review
- Revisiting the Role of Clathrin-Mediated Endoytosis in Synaptic Vesicle Recycling.Frontiers in cellular neuroscience · 2018Review
- Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network ofG3 (Bethesda, Md.) · 2017Article
- Article
- J domain independent functions of J proteins.Cell stress & chaperones · 2016Review
- Auxilin facilitates membrane traffic in the early secretory pathway.Molecular biology of the cell · 2016Article
- Swa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [URE3-1].Molecular microbiology · 2015Article
- Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.The Journal of biological chemistry · 2014Article
- Genome-wide expression analysis of HSP70 family genes in rice and identification of a cytosolic HSP70 gene highly induced under heat stress.Functional & integrative genomics · 2013Article
- Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones.Molecular bioSystems · 2012Article
- Phospholipid flippases: building asymmetric membranes and transport vesicles.Biochimica et biophysica acta · 2012Review
- Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Structure and activity of JAC1 J-domain implicate the involvement of the cochaperone activity with HSC70 in chloroplast photorelocation movement.Plant signaling & behavior · 2010Article
- The antidepressant sertraline targets intracellular vesiculogenic membranes in yeast.Genetics · 2010Article
- Photoreceptor IFT complexes containing chaperones, guanylyl cyclase 1 and rhodopsin.Traffic (Copenhagen, Denmark) · 2009Article
- The clathrin-binding motif and the J-domain of Drosophila Auxilin are essential for facilitating Notch ligand endocytosis.BMC developmental biology · 2008Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The auxilin family of J-domain proteins load Hsp70 onto clathrin-coated vesicles (CCVs) to drive uncoating. In vitro, auxilin function requires its ability to bind clathrin and stimulate Hsp70 ATPase activity via its J-domain. To test these requirements in vivo, we performed a mutational analysis of Swa2p, the yeast auxilin ortholog. Swa2p is a modular protein with three N-terminal clathrin-binding (CB) motifs, a ubiquitin association (UBA) domain, a tetratricopeptide repeat (TPR) domain, and a C-terminal J-domain. In vitro, clathrin binding is mediated by multiple weak interactions, but a Swa2p truncation lacking two CB motifs and the UBA domain retains nearly full function in vivo. Deletion of all CB motifs strongly abrogates clathrin disassembly but does not eliminate Swa2p function in vivo. Surprisingly, mutation of the invariant HPD motif within the J-domain to AAA only partially affects Swa2p function. Similarly, a TPR point mutation (G388R) causes a modest phenotype. However, Swa2p function is abolished when these TPR and J mutations are combined. The TPR and J-domains are not functionally redundant because deletion of either domain renders Swa2p nonfunctional. These data suggest that the TPR and J-domains collaborate in a bipartite interaction with Hsp70 to regulate its activity in clathrin disassembly.
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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.