Report for: Lysine Residue at Position 22 of the AID Protein Regulates Its Class Switch Activity

Title	Lysine Residue at Position 22 of the AID Protein Regulates Its Class Switch Activity
Published in	PLOS ONE, February 2012
DOI	10.1371/journal.pone.0030667
Pubmed ID	22363466
Authors	Roland Geisberger, Michael Huemer, Franz J. Gassner, Nadja Zaborsky, Alexander Egle, Richard Greil
Abstract	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.

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Other	3	19%

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