Tom Kerppola, Ph.D.

Professor, Biological Chemistry

Ofc: 3220C MSRB III

1150 W. Medical Center Drive

Ann Arbor, MI  48109-5606


(734) 764-3554


Biological Chemistry, Medical School

Areas of Interest

The Kerppola laboratory uses original experimental approaches to investigate molecular processes in living cells and to develop new therapies for cancers and cardiovascular diseases. Current areas of investigation in the laboratory include:

1.  Molecular interactions in living cells and animals.  We study interactions among proteins and other macromolecules in their normal cellular environments by visualizing the complexes they form in vivo.  We have developed imaging tools, including bimolecular fluorescence complementation (BiFC) analysis, that enable us to detect interactions among different macromolecules under native conditions, (1, 9).

2. Nucleoprotein complex binding specificity and dynamics.  We investigate the roles of transcription factor complexes in the control of gene expression.  We use a wide range of experimental approaches ranging from fluorescence assays in vitro, in cells and in animals to studies of genome-wide chromatin occupancy (1, 4).

3.  Protein modifications in living cells.  We investigate how post-translational modifications alter the functions of proteins in their normal environments by visualizing the modified conjugates in vivo.  We have developed imaging tools, including ubiquitin-mediated fluorescence complementation (UbFC) analysis, that enable us to selectively detect specific modified proteins in cells, (7, 8).

4.  Chromatin and epigenetic regulation.  We investigate how chromatin binding proteins bind to specific genomic regions and how their occupancy is maintained over multiple cell generations.  We have developed complementation approaches to visualize and purify specific chromatin-associated complexes by the isolation of BiFC-stabilized complexes (iBiSC) (1, 2, 6, 7).

5.  Transcription regulatory mechanisms.  We investigate how DNA and chromatin-binding proteins act in concert to regulate transcription.  We use high-throughput sequencing approaches to characterize the binding and regulatory specificities of combinations of interaction partners (2, 3, 4, 5, 6).

6.  Diseases and development.  Many of the studies in our laboratory focus on disease mechanisms and developmental programs.  These studies seek to develop new therapeutic approaches and to identify new relationships between development and responses to drugs and environmental chemicals (3, 5).


Published Articles or Reviews

1. Deng, H. and T. Kerppola, Visualization of dKeap1-CncC interaction on chromatin illumines cooperative, xenobiote-specific gene activation. Development  141: 3277-3288, doi: 10.1242/dev.110528, 2014.  PMCID: PMC4197530

2.  Cheng, B, Ren, X and Kerppola, TK. KAP1 represses differentiation-inducible genes in embryonic stem cells through cooperative binding with PRC1 and derepresses pluripotency-associated genes. Molecular and Cellular Biology 34: 2075-2091, 2014. PMCID: PMC4019052

3.  Deng, H and Kerppola, TK.  CncC and dKeap1 xenobiotic regulators interact on chromatin and coordinate Drosophila metamorphosis. PLoS Genetics e1003263, doi: 10.1371/journal.pgen.1003263. 2013.  PMCID: PMC3567155

4.  Burns, VE and Kerppola TK.  Opposite Orientations of a Transcription Factor Heterodimer Can Bind DNA Cooperatively with Interaction Partners but have Different Effects on Gene Transcription.  Journal of Biological Chemistry 287: 31833-31844, 2012.  PMCID: PMC3442517

5.  Bai, S and Kerppola, TK.  Opposing roles of FoxP1 and Nfat3 in transcriptional control of cardiomyocyte hypertrophy.  Molecular and Cellular Biology 31 (14): 3068-3080, doi: 10.1128/MCB.00925-10, 2011.  PMCID: PMC3133389

6.  Ren, X and Kerppola, TK. REST interacts with Cbx proteins and regulates polycomb repressive complex 1 occupancy at RE1 elements. Molecular and Cellular Biology 31:  2100-2110, 2011.  PMCID: PMC3133345

7.  Vincenz, C and Kerppola, TK. Different polycomb group CBX family proteins associate with distinct regions of chromatin using non-homologous protein sequences. Proceedings of the National Academy of Sciences U.S.A., 105: 16572-16577, 2008. PMCID: PMC2568982

8.  Fang, D and Kerppola, TK.  Ubiquitin-mediated fluorescence complementation reveals that Jun ubiquitinated by Itch/AIP4 is localized to endo-lysosomes. Proceedings of the National Academy of Sciences U.S.A, 101: 14782-14787, 2004. PMCID: PMC522008

9.  Hu, CD, and Kerppola, TK. Simultaneous visualization of interactions between multiple proteins in living cells using multicolor fluorescence complementation analysis. Nature Biotechnology, 21: 539-545, 2003. PMCID: PMC1820765

10.  Hu, CD, Chinenov, Y and Kerppola, TK.  Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Molecular Cell 9: 789-798, 2002. PMID: PMID: 11983170

For a list of publications from PubMed, click HERE

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