Daria Mochly-Rosen

Administrative Appointments

• Senior Associate Dean for Research, School of Medicine (2006 - present)
• Professor, Department of Chemical and Systems Biology (2001 - present)
• Chief, Division of Chemical Biology (2001 - 2002)
• Member, Neuroscience Institute at Stanford (2002 - present)
• Chair, Department of Molecular Pharmacology (2002 - 2006)
View All 8administrative appointments of Daria Mochly-Rosen

Honors and Awards

• The George D Smith Professor of Translational Medicine, School of medicine (2005)
• Reed-Hodgson Professor in Human Biology, Stanford University (1996-2001)

Professional Education

Postdoctoral Advisees

Grant Budas , Suresh Palaniyandi , Xin Qi , Nir Qvit

Graduate & Fellowship Program Affiliations

• Cancer Biology
• Chemical and Systems Biology

Web Site Links

• Mochly-Rosen Lab Site

Industry Relationships

Stanford is committed to ethical and transparent interactions with our industry partners. It is our policy to disclose payments of $5,000 or more, equity valued at $5,000 or more in a publicly traded company, or any equity in a privately held company, to physicians and scientists employed by Stanford University from companies or other commercial entities with which they interact as part of their professional activities. View Full Information

Research Interests

We are studying the mechanism of protein kinase C-mediated signal transduction in several disease models. Based on our recent data, we proposed a working hypothesis that activated PKC isozymes bind to intracellular receptor proteins located at different subcellular sites, and that these receptors differentially bind specific PKC isozymes. Evidence was obtained for the presence of intracellular receptor proteins that bind activated PKC. Binding of PKC to these proteins was concentration-dependent, saturable and specific, suggesting that these binding proteins are receptors for activated C-kinase, or "RACKs".

We have characterized and cloned several RACKs and identified domains in different PKC isozymes that are required for the specific association with these RACKs; these domains are distinct from the substrate binding site on PKC. On the basis of this information, together with computer modeling of crystal structures of the interacting proteins, we have identified novel isozyme-selective inhibitors that inhibit translocation and the consequent function of individual PKC isozymes. These inhibitors are fragments of PKC or RACKs that have 'dominant negative' activities on PKC binding to RACKs and on their activities, in vivo. In addition, we prepared synthetic peptides corresponding to the binding sites in PKC and RACKs. We are currently determining the effects of these isozyme-selective translocation inhibitors on a number of PKC-mediated cell functions in normal and diseased heart. These include cardiac and smooth muscle cell contraction, gene expression, hypertrophy, and response to and protection from ischemic insult.

Publications

• Centrosomal PKCbetaII and pericentrin are critical for human prostate cancer growth and angiogenesis. Kim J, Choi YL, Vallentin A, Hunrichs BS, Hellerstein MK, Peehl DM, Mochly-Rosen D. Cancer Res. 2008; 68 (16): 6831-9
• Sustained pharmacological inhibition of deltaPKC protects against hypertensive encephalopathy through prevention of blood-brain barrier breakdown in rats. Qi X, Inagaki K, Sobel RA, Mochly-Rosen D. J Clin Invest. 2008; 118 (1): 173-82
• Activation of aldehyde dehydrogenase-2 reduces ischemic damage to the heart. Chen CH, Budas GR, Churchill EN, Disatnik MH, Hurley TD, Mochly-Rosen D. Science. 2008; 321 (5895): 1493-5
• RBCK1, a protein kinase CbetaI (PKCbetaI)-interacting protein, regulates PKCbeta-dependent function. Vallentin A, Mochly-Rosen D. J Biol Chem. 2007; 282 (3): 1650-7
• Peptides derived from the C2 domain of protein kinase C epsilon (epsilon PKC) modulate epsilon PKC activity and identify potential protein-protein interaction surfaces. Brandman R, Disatnik MH, Churchill E, Mochly-Rosen D. J Biol Chem. 2007; 282 (6): 4113-23