Abstract:
: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. VCP methylation was abolished in three human VCP-KMT knockout cell lines generated with zinc-finger nucleases. Interestingly, VCP-KMT was recently reported to promote tumour metastasis, and indeed, VCP-KMT-deficient cells displayed reduced growth rate, migration and invasive potential. Finally, we present data indicating that VCP-KMT, calmodulin-lysine methyltransferase and eight uncharacterized proteins together constitute a novel human protein methyltransferase family. The present work provides new insights on protein methylation and its links to human disease.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Kernstock S,Davydova E,Jakobsson M,Moen A,Pettersen S,Mælandsmo GM,Egge-Jacobsen W,Falnes PØdoi
10.1038/ncomms2041subject
Has Abstractpub_date
2012-01-01 00:00:00pages
1038issn
2041-1723pii
ncomms2041journal_volume
3pub_type
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