The complexity of prokaryotic and, exceedingly, of eukaryotic cells, challenges the implementation of methodologies to determine causality and quantify intracellular dynamics. Although stochastic thermodynamics can be used to effectively quantify the dynamics of single proteins or complexes, there is no statistical approach that can be used to generalize subcellular microstates to determine the macrostates of a whole cell. Onsager reciprocity, a coupling between thermodynamic flows, has not been used systematically to quantify and establish causality among cellular dynamics. A prototypical thermodynamic profile of the cell is formulated as a model system to enable representation of its dynamics as force-driven thermodynamic flows. The explanatory potential of the methodology of thermodynamic reciprocity is demonstrated on molecular mechanisms in which coupling between internal fluxes is evident. Its predictive potential is then tested against mechanisms wherein coupling is unacknowledged, ruling out reciprocity between the contractile ring of the bacterial ortholog of tubulin, which facilitates the separation of dividing Escherichia colicells, and the bacterial actin ortholog, which polymerizes along the cell walls. In contrast, reciprocity is identified, albeit with a large margin of error, between the actomyosin ring, which facilitates the division of fission yeast cells and treadmilling longitudinal microtubules. Directly pertinent to the definition of the cell's prototypical thermodynamic profile, the reciprocity that was suggested between AMP-regulated kinase (AMPK) and mechanistic target of rapamycin (mTORC1) in the regulation of the cell cycle is confirmed. These findings support wider implementation of thermodynamic reciprocity to quantify and establish causal relationships among cellular dynamics.