Lysine methylation of VCP by a member of a novel human protein methyltransferase family.

@article{Kernstock2012LysineMO,
  title={Lysine methylation of VCP by a member of a novel human protein methyltransferase family.},
  author={Stefan Kernstock and Erna Davydova and Magnus E. Jakobsson and Anders Moen and Solveig J. Pettersen and Gunhild Mari M{\ae}landsmo and Wolfgang Egge-Jacobsen and P{\aa}l {\O}. Falnes},
  journal={Nature communications},
  year={2012},
  volume={3},
  pages={
          1038
        }
}
Valosin-containing protein (VCP, also called p97) is an essential and highly conserved adenosine triphosphate-dependent chaperone implicated in a wide range of cellular processes in eukaryotes, and mild VCP mutations can cause severe neurodegenerative disease. Here we show that mammalian VCP is trimethylated on Lys315 in a variety of cell lines and tissues, and that the previously uncharacterized protein METTL21D (denoted here as VCP lysine methyltransferase, VCP-KMT) is the responsible enzyme… 
Lysine Methylation of the Valosin-Containing Protein (VCP) Is Dispensable for Development and Survival of Mice
TLDR
The results show that VCPKMT is an enzyme required for methylation of K315 of VCP in vivo, but VCPkMT is not essential for development or survival under unstressed conditions.
Identification and Characterization of a Novel Human Methyltransferase Modulating Hsp70 Protein Function through Lysine Methylation*
TLDR
It is shown that trimethylation of HSPA8 (Hsc70) has functional consequences, as it alters the affinity of the chaperone for both the monomeric and fibrillar forms of the Parkinson disease-associated protein α-synuclein.
Human METTL20 Is a Mitochondrial Lysine Methyltransferase That Targets the β Subunit of Electron Transfer Flavoprotein (ETFβ) and Modulates Its Activity*
TLDR
The present study establishes METTL20 as the first human KMT localized to mitochondria and suggests that it may regulate cellular metabolism through modulating the interaction between its substrate ETFβ and dehydrogenases.
Elongation factor methyltransferase 3--a novel eukaryotic lysine methyltransferase.
Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function
TLDR
METTL18 is established as the second human histidine-specific protein MTase, and its functional relevance is demonstrated, indicating that METTL18-mediated methylation of RPL3 is important for optimal ribosome biogenesis and function.
A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A.
A System for Enzymatic Lysine Methylation in a Desired Sequence Context
TLDR
A versatile system for introducing lysine methylation into a desired peptide sequence is described, and the approach should be readily expandable for generating combinatorial libraries of methylated sequences.
Human FAM173A is a mitochondrial lysine-specific methyltransferase that targets adenine nucleotide translocase and affects mitochondrial respiration
TLDR
It is demonstrated that FAM173A is the long-sought KMT responsible for ANT methylation at Lys-52, and point out the functional significance of Lys- 52 methylation in ANT.
The activity of a yeast Family 16 methyltransferase, Efm2, is affected by a conserved tryptophan and its N‐terminal region
TLDR
It is shown that an active site‐associated tryptophan, invariant in Family 16 methyltransferases and at position 222 in Efm2, is important for methyltransferase activity and that Efm 2 can exist as an oligomer but that its N terminus is not necessary for oligomerisation to occur.
Methylation of human eukaryotic elongation factor alpha (eEF1A) by a member of a novel protein lysine methyltransferase family modulates mRNA translation
TLDR
It is demonstrated that an uncharacterized human 7BS MTase currently annotated as part of the endothelin converting enzyme 2, but which should be considered a separate enzyme efficiently methylates K36 in eukaryotic translation elongation factor 1 alpha (eEF1A) in vitro and in vivo.
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