Eric R. Strieter

Incorporation of Functional Proteins on Cellular Surfaces via Artificial Cell-Derived Vesicles (ACDVs) for Plasma Membrane Reprogramming

Shuai Gong, Jingyi Qiu, Fangying Huang, Jithu Krishna et autres

The complexity of cell surface proteins and their undruggable nature remain major challenges for functional modulation strategies such as small-molecule inhibition. Here, we present an artificial cell-derived vesicle (ACDV) approach that enables the direct delivery of functional proteins onto the cell surface, …

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Site-Specific Nanobody Inhibitors of the Proteasomal Deubiquitinase UCH37

Y. LI, Lin Hui Chang, Rishi Patel, Elizaveta I. Shestoperova et autres

Dysregulation of the ubiquitin (Ub) proteasome system (UPS) is linked to numerous human diseases, making its components, particularly deubiquitinases (DUBs), attractive therapeutic targets. UCH37 (also known as UCHL5), a proteasomal DUB, plays roles in protein degradation, DNA repair, and transcription and is …

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Computationally Driven Top-Down Mass Spectrometry of Ubiquitinated Proteins

Elizaveta I. Shestoperova, Daniil G. Ivanov, Eric R. Strieter

ABSTRACT Ubiquitination regulates numerous cellular processes through the attachment of polyubiquitin (Ub) chains that vary in linkage type, length, and branching topology. However, current mass spectrometry approaches cannot simultaneously define both the site of ubiquitination and the topology of the attached Ub …

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Hydrophilic α-Aryl-α-Diazoamides for Protein Esterification

Ronald T. Raines, Aniekan Okon, Anton Morgunov, Jin-Yi Yang et autres

Abstract Bioreversible protein esterification is a simple, customizable, and traceless strategy for the exogenous delivery of proteins into mammalian cells. Enabling this protein delivery strategy are α-aryl-α-diazoamides bearing a tolyl moiety. The aqueous solubility of the ensuing esterified protein is, however, often …

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Cytosolic Delivery of Functional Ubiquitin

JoLynn B. Giancola, Aniekan Okon, Y. LI, Eric R. Strieter et autres

ABSTRACT The proteostasis network involves complex protein signaling cascades. The tagging of proteins with ubiquitin is central to the degradation of cellular proteins, but understanding its exact role in processing proteins is complicated by the complexity and extent of its utilization within …

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Abstract 2421 Chain Branching by the NEDD4 Family Ubiquitin Ligases Stimulates Protein Degradation

Aidan Barich, Isabella Holt, Emma Werner, Anthony Daley et autres

The NEDD4 family of ubiquitin ligases targets a multitude of protein substrates for ubiquitination and degradation by the proteasome. However, most in vitro studies indicate that the NEDD4 family E3s have a preference for forming K63-linked chains, which typically are not associated …

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Optimized isolation of enzymatically active ubiquitin E3 ligase E6AP/UBE3A from mammalian cells

Johanna M. Schafer, Christine S. Muli, Rehab A Heikal, Marzena Dyba et autres

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Facile Access to Branched Multispecific Proteins

Aniekan Okon, Jin-Yi Yang, JoLynn B. Giancola, Oscar Molina et autres

Approaches that leverage orthogonal chemical reactions to generate protein-protein conjugates have expanded access to bespoke chimeras. Although the literature is replete with examples of the semisynthesis of bispecific proteins, few methods exist for the semisynthesis of protein conjugates of higher complexity (i.e., …

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Abstract 2148 "Chain Branching by NEDD4 Family Ubiquitin Ligases Regulates Protein Degradation"

Isabella Holt, Anthony Daley, Kayla Brennan, Yanfeng Li et autres

Ubiquitin chains are post-translational signals that regulate the stability, activity, and localization of eukaryotic proteins in a variety of ways. Recent studies indicate that ubiquitin chains can be branched and that branched chains impact the proteins they are attached to through mechanisms …

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Uncovering DUB Selectivity through an Ion Mobility-Based Assessment of Ubiquitin Chain Isomers

Elizaveta I. Shestoperova, Eric R. Strieter

Ubiquitination is a reversible post-translational modification that maintains cellular homeostasis and regulates protein turnover. Deubiquitinases (DUBs) are a large family of proteases that catalyze the removal of ubiquitin (Ub) along with the dismantling and editing of Ub chains. Assessing the activity and …

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Uncovering DUB Selectivity Through Ion-Mobility-Based Assessment of Ubiquitin Chain Isomers

Elizaveta I. Shestoperova, Eric R. Strieter

Ubiquitination is a reversible posttranslational modification that maintains cellular homeostasis and regulates protein turnover. Deubiquitinases (DUBs) are a large family of proteases that catalyze the removal of ubiquitin (Ub) along with the dismantling and editing of Ub chains. Assessing the activity and …

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Quantitative Analysis of Diubiquitin Isomers Using Ion Mobility Mass Spectrometry

Elizaveta I. Shestoperova, Daniil G. Ivanov, Eric R. Strieter

The diversity of ubiquitin modifications calls for methods to better characterize ubiquitin chain linkage, length, and morphology. Here, we use multiple linear regression analysis coupled with ion mobility mass spectrometry (IM-MS) to quantify the relative abundance of different ubiquitin dimer isomers. We …

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