Therefore, we could follow the fate of different proteins in the secretory pathway, without utilising radioactive isotopes or cycloheximide. The most novel aspect of our work is the use of the Halotag technology to determine how potentially harmful protein deposits form and grow in the secretory pathway. We show here that aggregates formation over time proceeds as deposition of newly made proteins on a pre-existing condensation core, resulting in a progressive increase of the clusters size. In this external shell of the aggregates, no mixing between new and old material is observed, suggesting that mDCH1 clusters are therefore rather “viscous” and grow mostly on the surface. However, given the limited resolution of confocal microscopy, we cannot determine if the newly deposited material can penetrate in the nucleation core of the RB. Accordingly, inhibiting microtubules decreased RB diffusion coefficient, indicating a partial role of microtubules in determining RB movements. Very interestingly, both small and big clusters displayed constrained mobility, which was not affected by Nocodazole. This observation suggests that an important constraining factor could be the ER membrane itself. Numerous questions remain to be answered: do different seeds coalesce together? What determines their size? What is the structural organization of these clusters? If their content is viscous, how does it distribute concentrically? How do cells dispose of RB? Extending the techniques described herein to super-resolution fluorescence microscopy could allow answering many of these relevant issues. Given the importance of protein aggregates, granules and clusters in storage diseases and also other regulatory processes our results describe a powerful tool for better visualizing and describing in vivo these events, being able to discriminate between old and young molecules in the same aggregate. Thus, this strategy is useful in order to reveal important mechanistic insights in the pathophysiology of ERSD and other disorders caused by proteotoxicity. Environmental stress disrupts homeostasis and can affect biological functions. Temperature has profound effects on the physical and chemical processes within biological systems. Variations in environmental temperature affect many properties and functions of biomolecules and structural components of cells, such as folding, assembly, activity, and stability of proteins ; structure and rigidity of lipids ; and fluidity and AZD6244 permeability of cell membranes. Rapid decrease in water temperature can lead to many physiological, behavioral, and fitness-related consequences in fish; even small changes in temperature adversely disturb cellular homeostasis and attenuate physiological performance. The adverse effects of temperature fluctuations are overcome and normal cellular functions during altered temperatures are maintained in some fish species via the evolution of versatile mechanisms that enable them to survive in extreme environments. Studies elucidating the mechanisms of temperature acclimation and responses to cold stress in fish have mainly been performed in freshwater fish. Under low temperature conditions, adaptive changes occur in the level.