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RanBPM associates with CD39 and modulates ecto-nucleotidase activity.
Yan Wu1, Xiaofeng Sun, Elzbieta Kaczmarek
1Liver Center, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.
The Biochemical Journal
|February 16, 2006
Summary
CD39, an enzyme regulating inflammation, interacts with RanBPM, a scaffolding protein. This binding affects CD39
Area of Science:
- Biochemistry
- Immunology
- Cell Biology
Background:
- CD39 (nucleoside triphosphate diphosphohydrolase 1) is an ecto-nucleotidase crucial for immune and vascular cell signaling in inflammation.
- The interaction of CD39 with other cellular proteins has not been previously established.
Purpose of the Study:
- To investigate potential interactions between CD39 and other proteins.
- To elucidate the functional consequences of any identified interactions on CD39 activity.
Main Methods:
- Yeast two-hybrid system to screen for CD39 interacting proteins.
- Co-immunoprecipitation in transfected mammalian cells to confirm protein complex formation.
- Analysis of NTPDase activity in COS-7 cells expressing CD39 and RanBPM.
Main Results:
- The N-terminus of CD39 was found to bind to RanBPM (Ran binding protein M).
- Complex formation between CD39 and RanBPM was confirmed in mammalian cells and endogenous co-expression in B-lymphocytes was observed.
- RanBPM co-expression significantly diminished the NTPDase activity of CD39, indicating functional regulation.
Conclusions:
- CD39 associates with the scaffolding protein RanBPM.
- This interaction has the potential to regulate CD39's catalytic activity.
- The CD39-RanBPM interaction may play a significant role in modulating extracellular nucleotide-mediated signaling pathways relevant to inflammation.