Aarhus University Seal / Aarhus Universitets segl

Poul Nissen

Flexible P-type ATPases interacting with the membrane

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Cation pumps and lipid flippases of the P-type ATPase family maintain electrochemical gradients and asymmetric lipid distributions across membranes, and offer significant insight of protein:membrane interactions. The sarcoplasmic reticulum Ca(2+)-ATPase features flexible and adaptive interactions with the surrounding membrane, while the Na(+),K(+)-ATPase complex is modulated by membrane components and a role for the γ-subunit as a stabilizer of a specific lipid interaction with the α-subunit has been proposed. The first crystal structure of a heavy-metal transporting ATPase shows a markedly amphipathic helix at the cytoplasmic membrane surface, highlighting this structure as a general motif of all P-type ATPases although with specialization to different membranes. Residues of central importance for the lipid flippase activity of the P4-type ATPase subfamily have been pinpointed by mutational studies, but the transport pathway and mechanism remain unknown.
Original languageEnglish
JournalCurrent Opinion in Structural Biology
Volume22
Issue4
Pages (from-to)491-499
Number of pages9
ISSN0959-440X
DOIs
Publication statusPublished - Aug 2012

See relations at Aarhus University Citationformats

ID: 48091841