Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 50, Pages 42888-42899Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.293852
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Funding
- Minerva Foundation
- Israel Science Foundation [ISF 996/06]
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Background: The alpha 2 isoform of Na, K-ATPase is unstable compared with alpha 1 and alpha 3. Results: Mutations in TM8-10 strongly stabilize alpha 2. A novel phospholipid antagonist selectively inactivates alpha 2, and mutations in TM8-10 protect against inactivation. Conclusion: A phosphatidylserine binding pocket within TM8-10 has been identified. Significance: Mechanistic insights into alpha 2 instability and a possible physiological role have been obtained.
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