Lysine residue at position 22 of the AID protein regulates its class switch activity.

ABSTRACT:

Background

Activation induced deaminase (AID) mediates class switch recombination and somatic hypermutation of immunoglobulin (Ig) genes in germinal centre B cells. In order to regulate its specific activity and as a means to keep off-target mutations low, several mechanisms have evolved, including binding to specific cofactors, phosphorylation and destabilization of nuclear AID protein. Although ubiquitination at lysine residues of AID is recognized as an essential step in initiating degradation of nuclear AID, any functional relevance of lysine modifications has remained elusive.

Methodology/principal findings

Here, we report functional implications of lysine modifications of the human AID protein by generating a panel of lysine to arginine mutants of AID and assessment of

SUBMITTER: Geisberger R 

PROVIDER: S-EPMC3282692 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature