Phosphorylation of Fanconi anemia protein, FANCA, is regulated by Akt kinase

  • Otsuki T
  • Nagashima T
  • Komatsu N
 et al. 
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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).

Author-supplied keywords

  • PKB/Akt
  • Phosphorylation
  • Serine/threonine

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  • Tetsuya Otsuki

  • Takahiro Nagashima

  • Norio Komatsu

  • Shin ichi Kobayashi

  • Keiya Ozawa

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