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Molecular Cell Short Article

Summary: Molecular Cell
Short Article
Evolution of Phosphorylation-Dependent Regulation
of Activation-Induced Cytidine Deaminase
Uttiya Basu,1 Yabin Wang,1 and Frederick W. Alt1,*
1Howard Hughes Medical Institute, The Children's Hospital, Harvard Medical School, and the Immune Disease Institute,
300 Longwood Avenue, Boston, MA 02115, USA
*Correspondence: alt@enders.tch.harvard.edu
DOI 10.1016/j.molcel.2008.08.019
Interaction of activation-induced cytidine deaminase
(AID) with replication protein A (RPA) has been
proposed to promote AID access to transcribed
double-stranded (ds) DNA during immunoglobulin
light chain and heavy chain class switch recombina-
tion (CSR). Mouse AID (mAID) interaction with RPA
and transcription-dependent dsDNA deamination
in vitro requires protein kinase A (PKA) phosphoryla-
tion at serine 38 (S38), and normal mAID CSR activity
depends on S38. However, zebrafish AID (zAID)


Source: Alt,, Frederick - Immune Disease Institute, Harvard University


Collections: Biology and Medicine