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Mazurkiewicz, L. E.

Publications and source records attributed to Mazurkiewicz, L. E..

2 recordsLinked to original sources

A self-organizing single-cell morphology circuit optimizes Podophrya collini predatory trap structure

Cellular structure self-organizes through an interplay between internal mechanisms and external cues. In predatory ciliates, structures that capture prey obtain the resources needed for their construction, creating feedback between environmental inputs and morphological outputs. Here, we describe a self-organizing single-cell morphology circuit that adaptively optimizes the predatory trap structure of the suctorian Podophrya collini. These trap structures ensnare large cellular targets using an array of straw-like tentacles that siphon out prey cytoplasm upon contact with their tips. We find that trap architecture scales anisotropically, favoring tentacle number over length, to construct traps that maximize capture probability for the resources on hand. Drug perturbations, transcriptomics, proteomics, and expansion microscopy define distinct molecular and structural requirements that regulate trap structure maintenance and tentacle biogenesis. We integrate these findings into a mathematical model that explains the adaptive scaling of the trap and that makes predictions we confirm experimentally. More broadly, this circuits architecture provides a general-purpose control logic for organizing the number and size of sub-cellular structures applicable to other natural and engineered cellular systems.

cell biology↗

Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases

Protein phosphorylation is dynamically regulated by the opposing activities of phosphowriter enzymes (kinases) and phosphoeraser enzymes (phosphatases and phospholyases). While significant progress has been made toward defining the sequences preferences of kinases, the selectivity of phosphoerasers has not been explored at scale. Here, we develop an experimental platform based on tandem mass spectrometry analysis of phosphoproteome-derived peptide libraries (PhosPropels) to map phosphoeraser activity across thousands of biologically relevant phosphosites. We extract positional residue preferences to rapidly define sequence motifs recognized by eight phosphoerasers spanning diverse species of origin, protein folds, and enzymatic mechanisms. Taking advantage of the throughput of our approach, we profiled 34 variants of the phosphothreonine lyase OspF from Shigella flexneri, uncovering an intrinsic preference for p38 and Erk MAP kinase activation loops and revealing the enzyme residues that influence its selectivity for phosphothreonine. Our results establish a general method for linking phosphorylation sites to the enzymes that remove them, providing a means to dissect a key component of cellular regulatory networks.

biochemistry↗