SIRT1, a cellular metabolic sensor, transcriptionally promotes sphingomyelin degradation in embryonic stem cells, which in turn modulates their membrane fluidity and neural differentiation.

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.

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.

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

Sirt3 functions as decrotonylase to regulate histone crotonylation dynamics.

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.

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.

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.