I received my Bachelor’s degree from the National Taiwan University (Taipei, Taiwan) in 2000. Later I went on to receive my PhD in 2012 from Stanford University (Stanford, California, USA). During my Ph.D. research, I has received the DOD breast cancer research program traineeship award in 2009. From my PhD study, I have published several high-impact papers about DNA damage response and cell cycle regulation on Molecular Cell, a prestigious journal in the cell & molecular biology field. After graduation, I worked as a Postdoc in Dr. Cimprich’s lab at Stanford University. In 2013, I moved to Harvard Medical School and joined the Laboratory of Systems Pharmacology as a postdoc.
I am currently in the Laboratory of Systems Pharmacology for my postdoctoral research. My work is to cultivate contemporary computational and experimental approaches for understanding drug-gene interactions in cancers, with specific focus on developing new imaging methods either for high-content/live-cell imaging in researching settings or multiplexed methods for clinical samples. My goal is to elucidate how genetic changes lead to heterogeneous responses of singling network, and to use this information for developing more effective therapeutic approaches.
B. Positions and Honors
Position and Employment
2013 - present
Postdoctoral Fellow. Laboratory of Systems Pharmacology, Harvard Medical School
2012 - 2013
Postdoctoral Fellow. Chemical and Systems biology, Stanford University
2004 – 2005
Research Assistant. National Taiwan University, Institute of Molecular Medicine, Taiwan .
DOD Breast Cancer Research Program Predoctoral Traineeship Award, sponsored by Department of Defense
Quantitative Chemical Biology Training Program, sponsored by Molecular Pharmacology, Stanford University
Outstanding Student Poster Presentation. Department of Chemical and Systems Biology Retreat, Stanford.
1999 – 2000
Undergraduate Research Fellowship sponsored by National Science Council, Taiwan
C. Contribution to Science
1. I developed a method to achieve high multiplexed single-cell imaging with cyclic immunofluorescence (CycIF), a simple and versatile procedure in which four-color staining alternates with chemical inactivation of fluorphores to progressively build a multi-channel image. I also demonstrate that live and fixed-cell imaging can be combined to exploit the advantages of both. In addition, CycIF data can be analyzed using conventional imaging software or the algorithms recently developed for high-dimensional data analysis & visualization. Altogether, this method will leads to many new venues for different research fields.
- Jia-Ren Lin, Mohammad Fallahi-Sichani, and Peter K Sorger. Highly multiplexed high-throughput imaging of single-cell using CycIF cyclic immunofluorescence, Nat. Comm. 2015, vol 6 8390
- Jia-Ren Lin, Mohammad Fallahi-Sichani, Jia-Yun Chen and Peter K Sorger. Cyclic Immunofluorescence (CycIF), A highly Multiplexed Method for Single-Cell Imaging, Cuurent Protocols in Chemical Biology 2016 in press
2. During my PhD and postdoc at Stanford, I study of the regulations of mutagenesis during damaged DNA replication, specifically focusing on the functions of post-replication repair (PRR) pathway. My research reveals a novel mechanism that cells differentially utilize HLTF and SHPRH for different forms of DNA damage through coordinating the two main branches of PRR to choose the proper bypass mechanism for minimizing mutagenesis. Furthermore, I also identified a new role for monoubiquitination in controlling Rad18 function and suggest that damage-specific deubiquitination promotes a switch from Rad18•Ub-Rad18 complexes to the Rad18-SHPRH complexes necessary for error-free lesion bypass in cells.
- Jia-Ren Lin, Zeman MK, Freire R, Cimprich KA. DNA Damage Alters the Ubiquitination State of Rad18 to Regulate Its Function and Its Assembly into DNA Damage Tolerance Complexes, J Cell biol. 2014 206(2): 183-197.
- Jia-Ren Lin, Zeman MK, Chen JY, Yee MC, Cimprich KA. SHPRH and HLTF act in a damage-specific manner to coordinate different forms of postreplication repair and prevent mutagenesis. Mol. Cell. 2011 42(2):237-49.
3. The other part of my PhD project was to study the process of oncogene-induced senescence with a focus on how cell-to-cell variability in oncogenic activity is linked to different cellular fates via time-lapse imaging and single-cell quantification. I helped to discover the roles of two disease-related genes, DyrK1a and Nek8 in regulating cell cyle length and DNA damage response during S-phase.
- Chen JY, Jia-Ren Lin, Tsai FC, and Meyer T. Dosage of Dyrk1a controls a decision for cell cycle exit by co-regulation of cyclin D1 and p21 levels. Mol. Cell. 2013 52(1):87-100.
- Choi HJ, Jia-Ren Lin, Vannier J, Saats GG, Kile AC, Paulsen RD, Manning DK, Beier DR, Giles RH, Boulton SJ, Cimprich KA. The ciliopathy-associated protein Nek8/NPHP9 acts with ATR to regulate the replication stress response. Mol. Cell. 2013 51(4):423-439.
- Chen JY, Jia-Ren Lin, Cimprich KA, Meyer T. A two dimensional ERK-AKT signaling code for an NGF-triggered cell fate decision. Mol. Cell. 2012 45(2):196-209.
4. My works in National Taiwan University was to investigations of the cellular function of two cytoskeleton associated genes, DAP kinase and a novel gene eIF3k. I identified that myosin regulatory light chain II as the in vitro and in vivo kinase substrate for DAP kinase. I also helped to reveals the function of eIF3k to relieve the caspase-sequestration effect of K8/K18, thereby increasing the availability of caspases to their non-keratin-residing substrates.
- Lin YM, Chen YR, Jia-Ren Lin, Wang WJ, Inoko A, Inagaki M, Wu YC, Chen RH. eIF3k regulates apoptosis in epithelial cells by releasing caspase 3 from keratin-containing inclusions. J Cell Sci. 2008 121(14):2382-93.
- Chen CH, Wang WJ, Kuo JC, Tsai HC, Jia-Ren Lin, and Chen RH. Bi-directional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK. EMBO J. 2005 24, 294-304.
- Kuo JC, Jia-Ren Lin, Staddon JM, Hosoya H, Chen RH. Uncoordinated regulation of stress fibers and focal adhesions by DAP kinase. J. Cell Sci. 2003 116, 4777-90