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

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 Commun

journal_title

Nature communications

authors

Kernstock S,Davydova E,Jakobsson M,Moen A,Pettersen S,Mælandsmo GM,Egge-Jacobsen W,Falnes PØ

doi

10.1038/ncomms2041

subject

Has Abstract

pub_date

2012-01-01 00:00:00

pages

1038

issn

2041-1723

pii

ncomms2041

journal_volume

3

pub_type

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