Structural and functional properties of the N- and C-terminal segments of the P4-ATPase phospholipid flippase ATP8A2.

ABSTRACT: ATP8A2 is a P4-ATPase that actively flips phosphatidylserine and to a lesser extent phosphatidylethanolamine across cell membranes to generate and maintain transmembrane phospholipid asymmetry. The importance of this flippase is evident in the finding that loss-of-function mutations in ATP8A2 are known to cause the neurodevelopmental disease known as cerebellar ataxia, intellectual disability, and dysequilibrium syndrome 4 (CAMRQ4) in humans and related neurodegenerative disorders in mice. Although significant progress has been made in understanding mechanisms underlying phospholipid binding and transport across the membrane domain, little is known about the structural and functional properties of the cytosolic N- and C-terminal segments of this flippase. In addition, there has been uncert

SUBMITTER: Matsell E 

PROVIDER: S-EPMC11750469 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature