A5071210616- Heat shock proteins research
- ATP Synthase and ATPases Research
- Enzyme Structure and Function
- Cytomegalovirus and herpesvirus research
- Calcium signaling and nucleotide metabolism
- Endoplasmic Reticulum Stress and Disease
- DNA Repair Mechanisms
- Genetics, Aging, and Longevity in Model Organisms
- Ubiquitin and proteasome pathways
- Computational Drug Discovery Methods
- Protein Structure and Dynamics
- Genetic and Kidney Cyst Diseases
- Hepatitis B Virus Studies
- Plant biochemistry and biosynthesis
- Muscle metabolism and nutrition
- thermodynamics and calorimetric analyses
- Venomous Animal Envenomation and Studies
- Bacterial Genetics and Biotechnology
- Renal cell carcinoma treatment
- Bacterial biofilms and quorum sensing
- Biochemical and Molecular Research
- Pancreatic function and diabetes
- Metabolism, Diabetes, and Cancer
- Microtubule and mitosis dynamics
- Calpain Protease Function and Regulation
University of Rochester
2020-2025
SUNY Upstate Medical University
2015-2024
State University of New York
2014-2023
Cancer Research Institute
2015-2016
SUNY College of Environmental Science and Forestry
2014
York University
2014
Article10 November 2017Open Access Source DataTransparent process Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients Mark R Woodford Department Urology, SUNY Upstate Medical University, Syracuse, NY, USA Cancer Center, Search for more papers by this author Rebecca A Sager Biochemistry Molecular Biology, Elijah Marris Diana M Dunn Adam Blanden Ryan L Murphy Nicholas Rensing Neurology, Washington University School Medicine, St. Louis,...
Significance The activity of many proteins is dependent on molecular chaperones and their accessory proteins, cochaperones. ability a cohort kinases, which are oncogenic, to transduce signals promoted by the heat shock protein 90 (Hsp90) chaperone Cdc37 cochaperone, requires removal phosphate from phosphatase 5 (PP5). We present crystal structure PP5 with trapped in active site. reveals how can associate different substrates previously unknown determinants specificity. Our findings show...
The molecular chaperone Hsp90 protects deregulated signaling proteins that are vital for tumor growth and survival. Tumors generally display sensitivity selectivity toward inhibitors; however, the mechanism underlying this phenotype remains undefined. We report mitotic checkpoint kinase Mps1 phosphorylates a conserved threonine residue in amino-domain of Hsp90. This, turn, regulates function by reducing ATPase activity while fostering association with clients, including Mps1. Phosphorylation...
Abstract Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase for its function it regulated by co-chaperones. Here we show that tumour suppressor FLCN client protein binding partners FNIP1/FNIP2 FNIPs decelerate cycle, facilitating interaction with Hsp90, consequently ensuring stability. compete activating co-chaperone Aha1 to thereby providing a...
ABSTRACT RAF1 is a key player in growth factor receptor signaling, which has been linked to multiple viral infections, including human cytomegalovirus (HCMV) infection. Although HCMV remains latent most individuals, it can cause acute infection immunocompromised populations, such as transplant recipients, neonates, and cancer patients. Current treatments are suboptimal, highlighting the need for novel therapies. Multiple points signaling pathway important infection, but relationship between...
The serine/threonine protein phosphatase 5 (PP5) regulates multiple cellular signaling networks. A number of factors, including heat shock 90 (Hsp90), promote the activation PP5. However, it is unclear whether post-translational modifications also influence PP5 activity. Here, we show an "on/off switch" mechanism for regulation. casein kinase 1δ (CK1δ) phosphorylates T362 in catalytic domain PP5, which activates and enhances activity independent Hsp90. Overexpression phosphomimetic T362E-PP5...
ABSTRACT There is a wealth of information on the genetic regulation and biochemical properties bacterial C 4 -dicarboxylate transport systems. In sharp contrast, there are far fewer studies describing assimilation 5 -dicarboxylates among bacteria. an effort to better our understanding this subject, we identified structural regulatory genes necessary for utilization α-ketoglutarate (α-KG) in Pseudomonas aeruginosa PAO1. The PA5530 gene, encoding putative dicarboxylate transporter, was found...
The serine/threonine protein phosphatase 5 (PP5) regulates hormone and stress-induced signaling networks. Unlike other phosphoprotein phosphatases, PP5 contains both regulatory catalytic domains is further regulated through post-translational modifications (PTMs). Here we identify that SUMOylation of K430 in the domain activity. Additionally, phosphorylation PP5-T362 pre-requisite for SUMOylation, suggesting ordered addition PTMs function cells. Using glucocorticoid receptor, a well known...
Human Cytomegalovirus (HCMV) infection modulates cellular metabolism to support viral replication. Calcium/calmodulin-dependent kinase (CaMKK) and AMP-activated protein (AMPK) regulate metabolic activation have been found be important for successful HCMV infection. Here, we explored the contributions that specific CaMKK isoforms AMPK subunit make toward Our results indicate various contribute in unique ways. For example, CaMKK1 is at a low multiplicity of infection, but dispensable earliest...
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes that plays a vital role protecting and maintaining the functional integrity of deregulated signaling proteins tumors. We have previously reported stability activity mitotic checkpoint kinase Mps1 depend on Hsp90. In turn, Mps1-mediated phosphorylation Hsp90 regulates its function for arrest. Cdc14-assisted dephosphorylation exit. Post-translational regulation also known as "Chaperone Code." Here, we demonstrate...
Heat Shock Protein 90 (Hsp90) is an essential chaperone that supports the function of a wide range signaling molecules. Hsp90 binds to suite co-chaperone proteins regulate through alteration intrinsic ATPase activity. Several studies have determined Aha1 be important whose binding modulated by phosphorylation, acetylation and SUMOylation [1], [2]. In this study, we applied quantitative affinity-purification mass spectrometry (AP-MS) proteomics understand how phosphorylation hAha1 at Y223...
You have accessJournal of UrologyKidney Cancer: Basic Research I1 Apr 2015MP39-02 OVEREXPRESSION OF MPS1 IN CLEAR CELL RENAL CARCINOMA (CCRCC) CONFERS TUMOR SELECTIVITY ON HEAT SHOCK PROTEIN-90 (HSP90) INHIBITORS Mourad Abouelleil, Diana Dunn, Mark Woodford, Sandra Jensen, Mahmoud Chehab, Alosh Madala, Tiffany Caza, Steve Landas, William G. Stetler-Stevenson, Len Neckers, Dimitra Bourboulia, Gennady Bratslavsky, and Mehdi Mollapour AbouelleilMourad Abouelleil More articles by this author ,...
You have accessJournal of UrologyKidney Cancer: Basic Research & Pathophysiology II1 Apr 2016MP85-13 FNIP CO-CHAPERONES PROTECT THE TUMOR SUPPRESSOR FLCN FROM UBIQUITINATION AND DEGRADATION IN PROTEASOME Mark Woodford, Diana Dunn, Adam Blanden, Stewart Loh, Dimitra Bourboulia, Laura Schmidt, W. Marston Linehan, Gennady Bratslavsky, and Mehdi Mollapour WoodfordMark Woodford More articles by this author , DunnDiana Dunn BlandenAdam Blanden LohStewart Loh BourbouliaDimitra Bourboulia...
The serine/threonine protein phosphatase 5 (PP5) regulates hormone and stress-induced signaling networks. Unlike other phosphoprotein phosphatases, PP5 contains both regulatory catalytic domains is further regulated through post-translational modifications (PTMs). Here we identified SUMOylation of K430 in the domain activity substrate release. Additionally, phosphorylation PP5-T362 pre-requisite for SUMOylation, suggesting ordered addition PTMs carefully function cells.Quantitative Förster...
Raf1 is a key player in growth factor receptor signaling, which has been linked to multiple viral infections, including Human Cytomegalovirus (HCMV) infection. Although HCMV remains latent most individuals, it can cause acute infection immunocompromised populations such as transplant recipients, neonates, and cancer patients. Current treatments are suboptimal, highlighting the need for novel treatments. Multiple points signaling pathway important infection, but relationship between Raf1,...
Abstract ChemInform is a weekly Abstracting Service, delivering concise information at glance that was extracted from about 100 leading journals. To access of an article which published elsewhere, please select “Full Text” option. The original trackable via the “References”
Abstract ChemInform is a weekly Abstracting Service, delivering concise information at glance that was extracted from about 100 leading journals. To access of an article which published elsewhere, please select “Full Text” option. The original trackable via the “References”