Joshua J. Hamey

1 month ago | cell.com | Joshua J. Hamey |Manan Shah |John Wade |Tara K. Bartolec |Kate Quinlan |Nicholas Williamson | +2 more

Keywordsribosometranslationlysine methylationmethyltransferasesubstrate specificityResearch topic(s)CP: Molecular biologyIntroductionFor over half a century, it has been known that the eukaryotic protein translational machinery is highly modified by protein methylation.1 Only in the last two decades, however, have enzymes catalyzing the methylation of ribosomes and translation factors been discovered.

Jan 16, 2024 | cell.com | Joshua J. Hamey |Marc Wilkins |Nicola M. Karakatsanis

Highlights Human histone demethylases are extensively phosphorylated, which can influence when and where they act on chromatin. Phosphorylation influences the function of histone demethylases via distinct mechanisms. Phosphorylation of histone demethylases occurs primarily in intrinsically disordered regions and at the interface of histone demethylase protein–protein interactions.

Jan 7, 2024 | jbc.org | Joshua J. Hamey |Amy Nguyen |Paige G. Pfeiffer |Marc Wilkins

AbstractTranslation elongation factor 1A (eEF1A) is an essential and highly conserved protein required for protein synthesis in eukaryotes. In both Saccharomyces cerevisiae and human, five different methyltransferases methylate specific residues on eEF1A, making eEF1A the eukaryotic protein targeted by the highest number of dedicated methyltransferases after histone H3.