ArticleJournal of proteome research2006
A proteomic screen identified stress-induced chaperone proteins as targets of Akt phosphorylation in mesangial cells.
Article in Journal of proteome research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Guaianolide dimer KGA-1002 targets GRP94 and triggers unfolded protein response-associated degradation of SKP2/AKT axis as a novel antihepatoma agent.Journal of advanced research · 2026Article
- Targeting chaperone modifications: Innovative approaches to cancer treatment.The Journal of biological chemistry · 2024Review
- HSP90 multi-functionality in cancer.Frontiers in immunology · 2024Review
- Low lamin A levels enhance confined cell migration and metastatic capacity in breast cancer.Oncogene · 2022Article
- Coordinated regulation of plant immunity by poly(ADP-ribosyl)ation and K63-linked ubiquitination.Molecular plant · 2021Article
- Heat Shock Proteins: Potential Modulators and Candidate Biomarkers of Peripartum Cardiomyopathy.Frontiers in cardiovascular medicine · 2021Review
- MAPK1 of Leishmania donovani interacts and phosphorylates HSP70 and HSP90 subunits of foldosome complex.Scientific reports · 2017Article
- Causes and consequences of nuclear envelope alterations in tumour progression.European journal of cell biology · 2016Review
- Alternative approaches to Hsp90 modulation for the treatment of cancer.Future medicinal chemistry · 2014Article
- Spatiotemporal dynamics of phosphorylation in lipid second messenger signaling.Molecular & cellular proteomics : MCP · 2013Review
- 4-Hydroxybenzyl alcohol confers neuroprotection through up-regulation of antioxidant protein expression.Neurochemical research · 2013Article
- Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code.Biochimica et biophysica acta · 2013Review
- Post-translational modifications of Hsp90 and their contributions to chaperone regulation.Biochimica et biophysica acta · 2012Review
- Article
- Differential proteome and phosphoproteome signatures in human T-lymphoblast cells induced by sirolimus.Cell proliferation · 2010Article
- Hsp90 phosphorylation, Wee1 and the cell cycle.Cell cycle (Georgetown, Tex.) · 2010Article
- Epigallocatechin-3-gallate (EGCG) attenuates inflammation in MRL/lpr mouse mesangial cells.Cellular & molecular immunology · 2010Article
- Identification of c-Src tyrosine kinase substrates in platelet-derived growth factor receptor signaling.Molecular oncology · 2009Article
- A truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 function.The Journal of biological chemistry · 2009Article
- Proteomic profiling of phosphoproteins and glycoproteins responsive to wild-type alpha-synuclein accumulation and aggregation.Biochimica et biophysica acta · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The serine-threonine kinase Akt regulates mesangial cell apoptosis, proliferation, and hypertrophy. To define Akt signaling pathways in mesangial cells, we performed a functional proteomic screen for rat mesangial cell proteins phosphorylated by Akt. A group of chaperone proteins, heat shock protein (Hsp) 70, Hsp90alpha, Hsp90beta, Glucose-regulated protein (Grp) Grp78, Grp94, and protein disulfide isomerase (PDI) were identified as potential Akt substrates by two techniques: (a) in vitro phosphorylation of mesangial cell lysate by recombinant active Akt followed by protein separation by SDS-PAGE or 2-DE and phosphoprotein identification by peptide mass fingerprinting using MALDI-MS, or (b) immunoblot analysis of proteins from PDGF-stimulated mesangial cells using an anti-Akt phospho-motif antibody. In vitro kinase reactions using recombinant proteins confirmed that Akt phosphorylates Hsp70, Hsp90alpha and beta, Grp94, and PDI. Immunoprecipitation of Akt from mesangial cell lysate coprecipitated Grp78 and Hsp70. PDGF stimulation of mesangial cells caused an acidic shift in the isoelectric point of Hsp70, Hsp90, and PDI that was dependent on PI-3K activity for Hsp70 and Hsp90. The data suggest that Akt-mediated phosphorylation of stress-induced chaperones represents a mechanism for regulation of chaperone function during mesangial cell responses to physiologic and pathologic stimuli.
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Registered trials
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