Identification of a Multiprotein "Motor" Complex Binding to Water Channel Aquaporin-2
|Title:||Identification of a Multiprotein "Motor" Complex Binding to Water Channel Aquaporin-2|
|Authors:||Noda, Yumi; Horikawa, Saburo; Katayama, Yoshifumi; Sasaki, Sei|
|Publisher:||Biochemical and Biophysical Research Communications|
|Date Published:||May 20, 2005|
This translation by the NDI Foundation is to assist the lay reader. To provide a clear, accessible interpretation of the original article, we eliminated or simplified some technical detail and complicated scientific language. We concentrated our translation on those aspects of the article dealing directly with NDI. The NDI Foundation thanks the researchers for their work toward understanding and more effectively treating this disorder.
© Copyright NDI Foundation 2007 (JC)
In that research, the research team identified two proteins that bind directly to AQP2: SPA-1 and actin. This finding led the researchers to speculate that these two proteins and AQP2 were part of a multi-protein complex that generates the force and motion necessary for AQP2 to make its trip.
In their most recent research, Noda, et al., analyzed a large amount of rat kidney to see if they could identify the proteins involved in the AQP2-associated protein complex. They found: ionized calcium binding adapter molecule 2, myosin regulatory light chain smooth muscle isoforms 2-A and 2-B, a-tropomyosin 5b, annexin A2 and A6, scinderin, gelsolin, a-actinin 4, a-II spectrin, and myosin heavy chain nonmuscle type A.
Since all the proteins identified are capable of binding with actin, the researchers speculate that these proteins may indirectly associate with AQP2 via actin. The researchers further speculate that these proteins form a complex that may provide this “motor” that drives the AQP2 to the cell membrane. They plan further research to clarify this.