Protein quality control research is “almost exclusively focused on heat shock proteins, which are ubiquitously present” up and down the evolutionary chain, Xiaolu Yang told BioWorld. But “for more sophisticated organisms, which we humans like to think we are, it’s a little odd that we still use the system that bacteria started with…. It seems like we should have something more. The TRIM system,” he added, “fills that gap.”

Protein quality control research is “almost exclusively focused on heat shock proteins, which are ubiquitously present” up and down the evolutionary chain, Xiaolu Yang told BioWorld. But “for more sophisticated organisms, which we humans like to think we are, it’s a little odd that we still use the system that bacteria started with…. It seems like we should have something more. The TRIM system,” he added, “fills that gap.”

TRIMs or tripartite motif proteins are a group of quality control proteins that are found only in animals. One of their functions is to add ubiquitin tags to proteins, marking them for transport to the proteasome system. TRIMs are part of the innate antiviral defense system. But in the July 27, 2023, issue of Science, Yang, who is a professor of cancer biology in the Perelman School of Medicine at the University of Pennsylvania, and his colleagues reported that TRIM11 interacts with tau protein in multiple ways that were beneficial in preventing tauopathies.

Researchers from Washington University in St. Louis reported data validating microtubule-binding region (MTBR) of tau containing the residue 243 (MTBR-tau243) as a new cerebrospinal fluid (CSF) biomarker specific for insoluble tau aggregates in Alzheimer’s disease (AD).

The inhibition of an enzyme associated with neurodegeneration processes reduced the toxic effect of tau, one of the proteins that damage neurons in Alzheimer’s disease (AD). A group of scientists from the University of Helsinki have shown in vitro and in animal models of AD how inhibition of the prolyl endopeptidase (PREP) enzyme reduced tau protein aggregations.

Scientists from Washington University in St. Louis have described a role for T cells in the neurodegeneration associated with the tau protein. Tau accumulation in the brain activated microglia. This signal triggered the activation of T cells in other parts of the body, attracting them to the brain. Once there, the interaction of these T cells and microglia produced the neuronal damage seen in Alzheimer’s disease and other tauopathies.

Looking ahead to potential commercialization of its late-stage tau PET imaging agent, Aprinoia Therapeutics Inc. has chosen to go public via a merger with special purpose acquisition company (SPAC) Ross Acquisition Corp. II in a deal that has an equity value of $280 million. The funding is aimed at getting candidate 18F-APN-1607 to the market in China.

A model of tauopathy developed in the worm nematode Caenorhabditis elegans was developed for investigating the mechanisms behind tauopathy development.