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While studying the transport of a multifunctional protein (GAPDH) out of cells we found that cells have evolved to devise multifunctionality not only in function of molecules but also in the process of their deployment. Our findings expose an interesting aspect of cellular housekeeping wherein cells utilize multiple routes to externalize a versatile protein and in the process utilize the penchant exhibited by moonlighting GAPDH to promiscuously interact with multiple protein partners, for sequestration and clearance of misfolded protein aggregates that accumulate during cellular stress. These findings highlight the occurrence of multifunctionality in cells not only in function of molecules but also in terms of cellular processes involving vital functions. This highly pleiotropic behavior is probably a consequence of natures fondness for optimal utilization of resources and building in redundancy for vital cellular processes. This phenomenon is similar to the practices in modern organizations wherein employees are called upon to multitask, for effecting economy, and also having in place substitute/alternate protocols in place to ensure continuity of essential functions in case of compromise of any one work process.
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This page is a summary of: Trafficking of a multifunctional protein by endosomal microautophagy: linking two independent unconventional secretory pathways, The FASEB Journal, January 2019, Wiley,
DOI: 10.1096/fj.201802102r.
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