Active nuclear import and cytoplasmic retention of activation-induced deaminase View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2009-05

AUTHORS

Anne-Marie Patenaude, Alexandre Orthwein, Yi Hu, Vanina A Campo, Bodil Kavli, Alejandro Buschiazzo, Javier M Di Noia

ABSTRACT

The enzyme activation-induced deaminase (AID) triggers antibody diversification in B cells by catalyzing deamination and consequently mutation of immunoglobulin genes. To minimize off-target deamination, AID is restrained by several regulatory mechanisms including nuclear exclusion, thought to be mediated exclusively by active nuclear export. Here we identify two other mechanisms involved in controlling AID subcellular localization. AID is unable to passively diffuse into the nucleus, despite its small size, and its nuclear entry requires active import mediated by a conformational nuclear localization signal. We also identify in its C terminus a determinant for AID cytoplasmic retention, which hampers diffusion to the nucleus, competes with nuclear import and is crucial for maintaining the predominantly cytoplasmic localization of AID in steady-state conditions. Blocking nuclear import alters the balance between these processes in favor of cytoplasmic retention, resulting in reduced isotype class switching. More... »

PAGES

517-527

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.1598

DOI

http://dx.doi.org/10.1038/nsmb.1598

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038443548

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19412186


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