Cenik Lab


Protein abundance is dictated by the complex interplay between the synthesis of a ‘message’ from DNA (RNA expression), the subsequent steps that are necessary to convert this ‘message’ into proteins, and the stability of these biomolecules. In a typical eukaryotic cell, the mRNA copy number of genes ranges from a single molecule to ~1000 molecules. However, the dynamic range of proteins in individual cells spans roughly from 100 to 1,000,000 copies. This discrepancy, along with the knowledge of mRNA and protein stability coefficients, implies that each mRNA molecule must be translated numerous times and that RNA expression alone only partially explains protein abundance variability. A significant portion of the variation in protein abundance can be attributed to translation efficiency, which refers to the number of proteins synthesized per mRNA molecule

Our long-term goal is to develop the necessary computational and experimental framework that will lead predictive models that explain how cells determine their protein abundance. Achieving this goal involves two major components: (1) higher-resolution and higher-precision measurements of various gene expression modalities, and (2) computational and theoretical advancements capable of integrating these quantitative measurements into cohesive, predictive frameworks.

Translation Efficiency Figure

Our Research Interests

Single cell ribosome profiling for characterizing translation in development, cancer and immunology

We developed a novel microfluidic isotachophoresis method (Ribo-ITP) to measure ribosome occupancy from ultra-low input samples including single cells.

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A computational framework to understand translational control

We develop machine learning models to integrate quantitative measurements of translation into cohesive, predictive frameworks.

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