WDR48 (WD repeat domain 48)

BRWD 3 ( bromodomain and WD repeat domain containing 3 )

Editorial: Signaling through WD-Repeat Proteins in Plants

Plants are sessile organisms that rely on appropriate signal-transduction responses in order to cope with the challenges imposed by their environment, and must be able to recognize potential damage or benefit to respond accordingly. These response mechanisms are mediated by specific sets of signal receptors, effector proteins interacting through scaffolding assemblies, second messengers, and tr...

Eukaryotic Chaperonins: Lubricating the Folding of WD-repeat Proteins

For most proteins of the eukaryotic cytosol, the folding pathways are still largely a mystery, even though many cytosolic chaperones have been identified, including multiple members of the heat shock protein (Hsp) 70 family, Hsp90 and the chaperonin, CCT/TRiC. Particularly puzzling has been the role of CCT, a distant cousin of the prokaryotic chaperonin GroEL, found in eukaryotes and archea. Gr...

Eukaryotic Chaperonins: Lubricating the Folding of WD-repeat Proteins Dispatch

For most proteins of the eukaryotic cytosol, the folding pathways are still largely a mystery, even though many cytosolic chaperones have been identified, including multiple members of the heat shock protein (Hsp) 70 family, Hsp90 and the chaperonin, CCT/TRiC. Particularly puzzling has been the role of CCT, a distant cousin of the prokaryotic chaperonin GroEL, found in eukaryotes and archea. Gr...

Molecular and biochemical characterization of three WD-repeat-domain-containing inositol polyphosphate 5-phosphatases in Arabidopsis thaliana.

Type II inositol polyphosphate 5-phosphatases (5PTases) in animals and yeast have been known to be important for regulating inositol and phospholipid signaling by hydrolyzing phosphate from both inositol polyphosphates and phosphoinositides. However, the molecular and biochemical properties of type II 5PTases in plants have not yet been studied. In this report, we show that three Arabidopsis ge...