Fig. 1.

The substrates of MYST acetyltransferases can be classified in distinct classes. The majority of the MYST acetyltransferases substrates are nuclear, although cytoplasmic substrates have been reported recently. The best studied MYST substrate class is histones, namely histones H4, H3, H2A and H2A variants. Histone acetylation by MYST proteins has impacts on transcription, DNA repair, DNA replication and other nuclear processes via histone modification crosstalks. Other typical substrates of MYST enzymes are subunits of MYST multiprotein complexes, including MYST proteins themselves. Aceytlation of MYST complex subunits mostly regulates complex stability and possibly target specificity. Another class of MYST substrates are transcription factors whose protein stability and transcription activity can be modified by MYST-dependent acetylation. Proteins involved in DNA damage response can also be acetylated by MYST proteins and this modification can increase kinase activity and checkpoint activation or the choice between cell cycle arrest and apoptosis. Finally, the only known cytoplasmic substrate of MYST enzymes so far is involved in glucose metabolism and acetylation of this substrate by a MYST enzyme regulates their involvement in lifespan elongation. See text for more information