Hundreds of proteins are involved in the DNA damage response but only three sensors for DSB were known but now SIRT6 is identified as a fourth DSB sensor.

SIRT1 deacetylates SIRT6 at K33 to facilitate DNA double-strand breaks-recognition, subsequent expansion and local chromatin remodeling.

The dramatic extension of lifespan in Sirt6-deficient mice by Trp53 haploinsufficiency suggests that SIRT6 has distinct biological function from SIRT1 in regulating p53 activity and preventing cells from senescence/apoptosis.

Mass spectroscopy, molecular modeling and/or molecular dynamics simulations reveal how acetylation regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation.

The ATM-SIRT6 axis integrates the DNA repair machinery to longevity-promoting pathways.

A posttranslational regulatory mechanism for a Ras family small GTPase could open up new directions to understand and control the Ras family of proteins that are important for physiology and diseases.

A new post-translational regulatory mechanism of K-Ras is identified, which expands the function of reversible protein lysine fatty acylation and offers new possibility to target the K-Ras oncoprotein.

In addition to its cytoplasmic role for translation, the seryl-tRNA synthetase also antagonizes the c-Myc transcription factor in the nucleus to transcriptionally repress the growth factor VEGFA and ensure proper development of the vasculature in vertebrates.

The small molecule Inauhzin possesses a dual targeting ability, and activates p53 by targeting two enzymes—SIRT1 and IMP dehydrogenase 2 (IMPDH2)—which are highly expressed in human cancers.

Sirt3 functions as decrotonylase to regulate histone crotonylation dynamics.