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Wucherer, K.

Publications and source records attributed to Wucherer, K..

2 recordsLinked to original sources

Intracellular K+ limits T cell exhaustion and preserves antitumor function

The cancer-killing activity of T cells is often compromised within tumors, allowing disease progression. We previously found that intratumoral elevations in extracellular K+ related to ongoing cell death constrained CD8+ T cell Akt-mTOR signaling and effector function (1,2). To alleviate K+ mediated T cell suppression, we pursued genetic means to lower intracellular K+. Transcriptomic analysis of CD8+ T cells demonstrated the Na+/K+ ATPase to be robustly and dynamically expressed. CRISPR-Cas9 mediated deletion of the catalytic alpha subunit of the Na+/K+ ATPase lowered intracellular K+ but produced tonic hyperactivity in multiple signal transduction cascades along with the acquisition of co-inhibitory receptors and terminal differentiation in mouse and human CD8+ T cells. Mechanistically, Na+/K+ ATPase disruption led to ROS accumulation due to depletion of intracellular K+ in T cells. Antioxidant treatment or high K+ media prevented Atp1a1 deficient T cells from exhausted T (TEx) cell formation. Consistent with transcriptional and proteomic data suggesting a TEx cell phenotype, T cells lacking Atp1a1 had compromised persistence and antitumor activity in a syngeneic model of orthotopic murine melanoma. Translational application of these findings will include efforts to lower intracellular K+ while limiting ROS accumulation within tumor specific T cells. SynopsisHigh extracellular K+ ({uparrow}[K+]e) is found within tumors and suppresses T cell effector function. Collier et al. find that deletion of the Na+/K+ ATPase in T cells lowers intracellular K+ and promotes ROS accumulation, tonic signal transduction and T cell exhaustion owing to ROS accumulation. Engineering T cell ion transport is an important consideration for cancer immunotherapy.

immunology↗

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIP

Microtubule-associated protein tau (MAPT/tau) accumulates in a family of neurodegenerative diseases, including Alzheimers disease (AD). In disease, tau is aberrantly modified by post-translational modifications (PTMs), including hyper-phosphorylation. However, it is often unclear which of these PTMs contribute to taus accumulation or what mechanisms might be involved. To explore these questions, we focused on a cleaved proteoform of tau (tauC3), which selectively accumulates in AD and was recently shown to be degraded by its direct binding to the E3 ubiquitin ligase, CHIP. Here, we find that phosphorylation of tauC3 at a single residue, pS416, is sufficient to block its interaction with CHIP. A co-crystal structure of CHIP bound to the C-terminus of tauC3 revealed the mechanism of this clash and allowed design of a mutation (CHIPD134A) that partially restores binding and turnover of pS416 tauC3. We find that pS416 is produced by the known AD-associated kinase, MARK2/Par-1b, providing a potential link to disease. In further support of this idea, an antibody against pS416 co-localizes with tauC3 in degenerative neurons within the hippocampus of AD patients. Together, these studies suggest a discrete molecular mechanism for how phosphorylation at a specific site contributes to accumulation of an important tau proteoform.

biochemistry↗