ArticleMolecular biology of the cell2011
Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- Wiring of cellular proteostasis by J-domain proteins.Cell stress & chaperones · 2026Review
- MAGMAS Inhibition Enhances Temozolomide Efficacy in Chemotherapy-Resistant Glioblastoma Models.Cancer research communications · 2026Article
- mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Presequence translocase-associated motor subunits of the mitochondrial protein import apparatus are dual-targeted to mitochondria and plastids.Frontiers in plant science · 2022Article
- Expansion of the evolutionarily conserved network of J-domain proteins in the Arabidopsis mitochondrial import complex.Plant molecular biology · 2021Article
- Redox-Mediated Regulation of Mitochondrial Biogenesis, Dynamics, and Respiratory Chain Assembly in Yeast and Human Cells.Frontiers in cell and developmental biology · 2021Review
- Skeletal Phenotypes Due to Abnormalities in Mitochondrial Protein Homeostasis and Import.International journal of molecular sciences · 2020Review
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- Common functions of the chloroplast and mitochondrial co-chaperones cpDnaJL (CDF1) and mtDnaJ (PAM16) in protein import and ROS scavenging in Arabidopsis thaliana.Communicative & integrative biology · 2016Review
- The role and significance of potential lipid-binding regions in the mitochondrial protein import motor: an in-depth in silico study.3 Biotech · 2015Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK.Frontiers in molecular biosciences · 2014Article
- Real-time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET.The EMBO journal · 2013Article
- Sequential duplications of an ancient member of the DnaJ-family expanded the functional chaperone network in the eukaryotic cytosol.Molecular biology and evolution · 2013Article
- ERdj3 regulates BiP occupancy in living cells.Journal of cell science · 2013Article
- Magmas overexpression inhibits staurosporine induced apoptosis in rat pituitary adenoma cell lines.PloS one · 2013Article
- Comparative analysis of putative orthologues of mitochondrial import motor subunit: Pam18 and Pam16 in plants.PloS one · 2013Article
- Mitochondrial protein synthesis, import, and assembly.Genetics · 2012Article
- Mechanisms of protein sorting in mitochondria.Cold Spring Harbor perspectives in biology · 2012Review
- Essential role of Drosophila black-pearl is mediated by its effects on mitochondrial respiration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The heat-shock protein 70 (Hsp70)-based import motor, associated with the translocon on the matrix side of the mitochondrial inner membrane, drives translocation of proteins via cycles of binding and release. Stimulation of Hsp70's ATPase activity by the translocon-associated J-protein Pam18 is critical for this process. Pam18 forms a heterodimer with the structurally related protein Pam16, via their J-type domains. This interaction has been proposed to perform a critical regulatory function, inhibiting the ATPase stimulatory activity of Pam18. Using biochemical and genetic assays, we tested this hypothesis by assessing the in vivo function of Pam18 variants having altered abilities to stimulate Hsp70's ATPase activity. The observed pattern of genetic interactions was opposite from that predicted if the heterodimer serves an inhibitory function; instead the pattern was consistent with that of mutations known to cause reduction in the stability of the heterodimer. Analysis of a previously uncharacterized region of Pam16 revealed its requirement for formation of an active Pam18:Pam16 complex able to stimulate Hsp70's ATPase activity. Together, our data are consistent with the idea that Pam18 and Pam16 form a stable heterodimer and that the critical role of the Pam18:Pam16 interaction is the physical tethering of Pam18 to the translocon via its interaction with Pam16.
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