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Tachiki, J.

Publications and source records attributed to Tachiki, J..

2 recordsLinked to original sources

The KAT2 Acetyltransferase PCAF-1 Couples Stress-Responsive Transcription to Proteostasis and Longevity

Aging erodes the capacity of cells to sense stress and maintain a functional proteome. Lysine acetyltransferases can link stress signals to gene expression, but whether boosting the activity of a single acetyltransferase can enhance stress responses to protect the aging proteome and extend healthspan remains unknown. Here we show that increasing the dosage of PCAF-1, the sole KAT2 family acetyltransferase in Caenorhabditis elegans, is sufficient to extend lifespan, preserve healthspan, and reprogram stress-responsive transcription. This program is conserved; mammalian orthologs of PCAF-1-induced genes are enriched among transcripts that decline upon KAT2A and KAT2B depletion. PCAF-1 strengthens inducible stress responses, attenuates the age-dependent decline in proteasomal degradation, and limits protein aggregation in C. elegans models of human neurodegenerative diseases, while preserving motility and survival. Mechanistically, PCAF-1 drives DAF-16/FOXO activation, and DAF-16 is required for both PCAF-1-dependent longevity and for protection against polyglutamine aggregation. These findings reveal a previously unrecognized mechanism by which KAT2 acetyltransferases promote longevity, positioning KAT2s as potential tunable regulators of proteostasis and healthspan during aging.

molecular biology↗

Coordination of Anle138b to Silver Results in Selective Reduction of a C-terminal truncated Alpha-synuclein Protein and Increased Aggregate Size

Parkinsons disease (PD) is a prevalent age-related neurodegenerative syndrome, partially thought to be caused by a decrease in alpha-synuclein proteostasis. Anle138b = 5-(1,3-benzodioxol-5-yl)-3-(3-bromophenyl)-1H-pyrazole (HL), is undergoing clinical trials as a promising mitigator of alpha-synuclein aggregation. Because complexation to metals is known to modulate the activity of several drugs, we have prepared and characterized: H2L(ClO4), [CuI({micro}-L)]3, and [AgI({micro}-L)]3. To better understand the bioviability of these compounds, we monitored their effects in a cell culture model of alpha-synuclein protein aggregation using human alpha-synuclein pre-formed fibrils (PFFs). Using two different anti-alpha-synuclein antibodies, our data suggests that [AgI({micro}-L)]3 decreases a C-terminal truncated protein that is approximately 12.4 kDa, as well as increases the size and alters the shape of PFF-induced aggregates. This indicates that [AgI({micro}-L)]3 impacts aggregation in a manner different from HL and may serve as a novel tool for studying C-terminal truncation related aggregation chemistry. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=101 SRC="FIGDIR/small/679869v1_ufig1.gif" ALT="Figure 1"> View larger version (18K): org.highwire.dtl.DTLVardef@4bbda5org.highwire.dtl.DTLVardef@8fc0b7org.highwire.dtl.DTLVardef@1b561f5org.highwire.dtl.DTLVardef@1322902_HPS_FORMAT_FIGEXP M_FIG C_FIG

biochemistry↗