Phsphorylation of the Fanconi anemia complementation group A (FANCA) protein is thought to be important for the function of the FA pathway. However, the kinase for FANCA (so-called FANCA-PK) remains to be identified. FANCA has a consensus sequence for Akt kinase near serine 1149 (Ser1149), suggesting that Akt can phosphorylate FANCA. We performed in vitro kinase assays using as substrate either a GST-fusion wild-type (WT) FANCA fragment or a GST-fusion FANCA fragment containing a mutation from serine to alanine at 1149 (FANCA-S1149A). These experiments confirmed that FANCA is phosphorylated at Ser 1149, in vitro. However, 32P-orthophosphate labeling experiments revealed that FANCA-S1149A was more efficiently phosphorylated than WT-FANCA. Furthermore, phosphorylation of wild-type FANCA was blocked by coexpression of a constitutively active (CA)-Akt and enhanced by a dominant-negative (DN) Akt. Our results suggest that Akt is a negative regulator of FANCA phosphorylation. © 2002 Elsevier Science (USA).
CITATION STYLE
Otsuki, T., Nagashima, T., Komatsu, N., Kirito, K., Kobayashi, S. ichi, Ozawa, K., … Liu, J. M. (2002). Phosphorylation of Fanconi anemia protein, FANCA, is regulated by Akt kinase. Biochemical and Biophysical Research Communications, 291(3), 628–634. https://doi.org/10.1006/bbrc.2002.6504
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