Ubiquitylation is a highly controlled post-translational modification of proteins, in which proteins are conjugated either with monoubiquitin or polyubiquitin chains. Ubiquitin modifications on target proteins are recognized by ubiquitin-binding domains, which are found in several effector proteins. We study the function and structure of the Toll-interacting protein (Tollip), which contains the C2 and CUE ubiquitin-binding domains and participates in the innate immune signaling pathway and endosomal protein trafficking.
The Wnt-dependent, b-catenin-independent pathway modulates cell movement and behavior. A downstream regulator of this signaling pathway is Dishevelled (Dvl), which among other multiple interactions, binds to the Frizzled receptor and the plasma membrane via phosphatidic acid (PA) in a mechanism proposed to be pH dependent. We defined the structural and functional basis of PA recognition by the Dvl2 DEP domain. We also established that PA binding by the Dvl2 DEP domain is pH-dependent and resembles the mechanism of PA deprotonation
Platelets form a clump at the site of vascular injury to stop bleeding. One negative regulator of platelet aggregation is Disabled-2 (Dab2), a protein released to the extracellular surface upon platelet activation. Dab2 inhibits platelet aggregation by competing with fibrinogen for alphaIIb-beta3 integrin receptor binding. The inhibitory role of Dab2 depends on its recognition to sulfatides, sphingolipids found on the platelet surface, which interact with coagulation proteins, playing a major role in haemostasis.
|Nhyira Annan||Visiting Student|
|Kevin Chen||Visiting Student|
|Meredith Crews||Visiting Student|
|Evan Littleton||Visiting Student|
|Wei Song||Visiting Student|
|Tuo-Xian Tang||Visiting Student|
|Robert Wallace||Visiting Student|
|Wen Xiong||Visiting Student|