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Williams syndrome transcription factor (WSTF) has emerged as an incredibly versatile nuclear protein. WSTF and the ATP-dependent chromatin remodeling complexes in which it exists, WINAC, WICH, and B-WICH, have been studied in a variety of organisms. This research has revealed roles for WSTF in a number of diverse molecular events. WSTF function includes chromatin assembly, RNA polymerase I and III gene regulation, vitamin D metabolism, and DNA repair. In addition to functioning as a subunit of several ATP-dependent chromatin remodeling complexes, WSTF binds specifically to acetylated histones and is itself a histone kinase as well as a target of phosphorylation. This review will describe the three known WSTF-containing complexes and discuss their various roles as well as mechanisms of regulating WSTF activity.

Since the publication of this review, there have been retractions of papers from the Sikeagi Kato lab cited in this review (http:// retractionwatch.com/category/shigeaki-kato/). The existence of the WINAC complex (and thus its attributed activities) is now in doubt, thus readers should disregard the section of this review that is focused onWINAC. This includes the role ofWINAC in vitamin D receptor (VDR)-dependent gene regulation, H3K14 binding by WSTF, and MAPK phosphorylation of WSTF and subsequent effects on complex formation. The authors of this review were disappointed to learn of these retractions and ask the readers to take note of the other excellent research cited in this review, and to not let themisconduct of one laboratory color their perceptions of other work in this field.