ArticleCell stress & chaperones2009
RDJ2 (DNAJA2) chaperones neural G protein signaling pathways.
Article in Cell stress & chaperones, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Trial
- DNAJA: emerging targets for anti-tumor therapy.Future oncology (London, England) · 2025Review
- Selective Binding of HSC70 and its Co-Chaperones to Structural Hotspots on CFTR.Scientific reports · 2020Article
- Hsp70 and DNAJA2 limit CFTR levels through degradation.PloS one · 2019Article
- Hsp70/J-protein machinery from Glossina morsitans morsitans, vector of African trypanosomiasis.PloS one · 2017Article
- Formation of chimeric genes by copy-number variation as a mutational mechanism in schizophrenia.American journal of human genetics · 2013Article
- The large conductance, calcium-activated K+ (BK) channel is regulated by cysteine string protein.Scientific reports · 2013Article
- The DNAJA2 substrate release mechanism is essential for chaperone-mediated folding.The Journal of biological chemistry · 2012Article
- Article
- Mutations in DNAJC5, encoding cysteine-string protein alpha, cause autosomal-dominant adult-onset neuronal ceroid lipofuscinosis.American journal of human genetics · 2011Article
- Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Progress in neurobiology · 2010Review
- Quercetin targets cysteine string protein (CSPalpha) and impairs synaptic transmission.PloS one · 2010Article
- Functional role of J domain of cysteine string protein in Ca2+-dependent secretion from acinar cells.American journal of physiology. Gastrointestinal and liver physiology · 2009Article
- Hsp40 couples with the CSPalpha chaperone complex upon induction of the heat shock response.PloS one · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A number of structurally divergent proteins with J domains, called J proteins, interact with and activate the ATPase of Hsp70s, thereby harnessing the ATPase activity for conformational work on target proteins. The precise role of most mammalian J proteins remains undefined. In this paper, we demonstrate that transient expression of the J protein, Rdj2, in HEK 293 cells increased cellular cyclic adenosine monophosphate (cAMP) levels in the presence of the beta-adrenergic agonist isoproterenol. In CNS-derived catecholaminergic neuronal cell line (CAD) neuroblastoma cells, expression of Rdj2 increased isoproterenol-stimulated phosphorylation of cAMP response element binding protein (CREB). Moreover, we have characterized the binding properties of Rdj2 and observed a direct interaction between Rdj2 and receptor-coupled trimeric GTP-binding proteins (G proteins). We further show that the composition of the Rdj2-chaperone complex and the cysteine string protein (CSPalpha)-chaperone complex, another J protein, is distinct. Our data demonstrate that Rdj2 modulates G protein signaling and further suggest that chaperoning G proteins is an emerging theme of the J protein network.
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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.