Richard B. Jones, PhD

Appointments:

Assistant Professor
Ben May Department for Cancer Research
Institute for Genomics and Systems
     Biology

Committee on Cancer Biology
Committee on Genetics

Education:

Ph.D., Alkek Institute for Biosciences
     and Technology, Texas A&M
     University, 2000

B.S. Biochemistry, Indiana University, 1994

Contact:

Phone:  (773) 702-2185

Lab:       (773) 256-9397

Fax:       (773) 702-4476

E-Mail:
rjones@huggins.bsd.uchicago.edu

Address:

The University of Chicago
GCIS W306
924 East 57th Street
Chicago, Illinois 60637

Related Research Interests:

Cancer Genetics

Cell Cycle

Cell Differentiation/Development

Cellular Interactions


Diabetes

Drug Discovery

Gene Regulation/Expression

Insulin Action

Metastatic Progression/Angiogenesis

Pharmacogenetics


Signal Transduction


Systems Biology

Tumor Biology/Immunology/Immunotherapy

Wound Healing

Richard B. Jones, Ph.D.


Focused Systems-Level Analyses of Cellular Signal Transduction

Research Summary

In order for living creatures to progress from single cells to multi-cellular tissues, organs, and ultimately to whole organisms, they must utilize complex autocrine, paracrine, and endocrine communication mechanisms that we are only beginning to understand at the molecular level.  While large scale analyses of cellular, tissue-level, and whole organism gene expression patterns have been performed in a scalable, systematic, and high-throughput manner with the DNA microarray and other platforms, the analysis of dynamic protein signaling networks has proven a much greater technological challenge.  At one extreme, cell biologists have examined total protein abundance and post-translational modification state from whole cells and tissues while at the other extreme biochemists and biophysicists have studied how a single post-translational modification can give rise to a change in protein structure and function.  The focus of our laboratory lies at the interface between these extremes and is the result of the belief that the use of technological approaches at the interface of scientific disciplines and scales will result in paradigm-shifting systems-level insights into fundamental biological processes and will simultaneously result in the development of tools with wide ranging applicability to cancer and other clinically relevant biology. 

Toward this end, we are utilizing protein micro-array, mass spectrometric, and cell biological tools to query both the theoretical biophysical nature of protein-protein interaction connectivity as well as the dynamics of cellular protein abundance, post-translational modification, and interaction connectivity.  We are focusing our efforts primarily on those interactions and modifications that would not be easily addressed using traditional yeast two hybrid methodologies.  Our goal is to gain a better understanding of the modular signaling molecules whose location, abundance, and modification state underlie cell growth, migration, differentiation, and cell death: These processes lie at the heart of cancer biology and an understanding of these processes at the molecular level should enable the identification of many new therapeutic targets. 

We are very interested in receiving applications from motivated students and postdoctoral researchers who wish to work at the interface of Biology, Chemistry, Physics, and Mathematics to better understand the signal transduction mechanisms that result in cancer, diabetes, and other human disease.


Selected Papers

Yu C, Wang F, Kan M, Jin C, Jones RB, Weinstein M, Deng CX, McKeehan WL. (2000). Elevated Cholesterol Metabolism and Bile Acid Synthesis in Mice Lacking Membrane Tyrosine Kinase Receptor FGFR4. Journal of Biological Chemistry. 275:15482-15489.

Jones RB, Wang F, Luo Y, Yu C, Jin C, Suzuki T, Kan M, McKeehan WL. (2001). The Nonsense-Mediated Decay Pathway and Mutually Exclusive Expression of Alternatively Spliced FGFR2IIIb and IIIc mRNAs. Journal of Biological Chemistry. 276:4158-4167.

Jones RB, Carstens RP, Luo Y, McKeehan WL. (2001). 5'- and 3'-terminal Nucleotides in the FGFR2 ISAR Splicing Element Core Have Overlapping Roles in Exon IIIb Activation and Exon IIIc Repression. Nucleic Acids Research. 29:3557-3565.

Ye S, Luo Y, Lu W, Jones RB, Linhardt RJ, Capila I, Toida T, Kan M, Pelletier H, McKeehan WL. (2001). Structural Basis for Interaction of FGF-1, FGF-2, and FGF-7 with Different Heparan Sulfate Motifs. Biochemistry 40:14429-14439.

Jones RB, Gordus AG, Krall J, MacBeath G. (2006). A Quantitative Protein Interaction Network for the ErbB Receptors Using Protein Microarrays. Nature. 439(7073):168-74.

Newman EA, Muh SJ, Hovhannisyan RH, Warzecha CC, Jones RB, McKeehan WL and Carstens RP. (2006). Identification of RNA-binding proteins that regulate FGFR2 splicing through the use of sensitive and specific dual color fluorescence minigene assays. RNA. 12: 1129-1141.

 

 

Faculty and Research

Programs

Cancer Biology


CCB

Immunology


COI

Microbiology


COM

Molecular Metabolism
and Nutrition


CMMN

Molecular Pathogenesis and
Molecular Medicine


MPMM