TY - JOUR
T1 - Fast-forward on P-type ATPases
T2 - recent advances on structure and function
AU - Stock, Charlott
AU - Heger, Tomás
AU - Hansen, Sara Basse
AU - Larsen, Sigrid Thirup
AU - Habeck, Michael
AU - Dieudonné, Thibaud Louis Antoine
AU - Driller, Ronja
AU - Nissen, Poul
PY - 2023/6
Y1 - 2023/6
N2 - P-type ATPase are present in nearly all organisms. They maintain electrochemical gradients for many solutes, in particular ions, they control membrane lipid asymmetry, and are crucial components of intricate signaling networks. All P-type ATPases share a common topology with a transmembrane and three cytoplasmic domains and their transport cycle follows a general scheme — the Post-Albers-cycle. Recently, P-type ATPase research has been advanced most significantly by the technological advancements in cryo-EM analysis, which has elucidated many new P-type ATPase structures and mechanisms and revealed several new ways of regulation. In this review, we highlight the progress of the field and focus on special features that are present in the five subfamilies. Hence, we outline the new intersubunit transport model of KdpFABC, the ways in which heavy metal pumps have evolved to accommodate various substrates, the strategies Ca
2+ pumps utilize to adapt to different environmental needs, the intricate molecular builds of the ion binding sites in Na,K- and H,K-ATPases, the remarkable hexameric assembly of fungal proton pumps, the many ways in which P4-ATPase lipid flippases are regulated, and finally the deorphanization of P5 pumps. Interestingly many of the described features are found in more than one of the five subfamilies, and mixed and matched together to provide optimal function and precise regulation.
AB - P-type ATPase are present in nearly all organisms. They maintain electrochemical gradients for many solutes, in particular ions, they control membrane lipid asymmetry, and are crucial components of intricate signaling networks. All P-type ATPases share a common topology with a transmembrane and three cytoplasmic domains and their transport cycle follows a general scheme — the Post-Albers-cycle. Recently, P-type ATPase research has been advanced most significantly by the technological advancements in cryo-EM analysis, which has elucidated many new P-type ATPase structures and mechanisms and revealed several new ways of regulation. In this review, we highlight the progress of the field and focus on special features that are present in the five subfamilies. Hence, we outline the new intersubunit transport model of KdpFABC, the ways in which heavy metal pumps have evolved to accommodate various substrates, the strategies Ca
2+ pumps utilize to adapt to different environmental needs, the intricate molecular builds of the ion binding sites in Na,K- and H,K-ATPases, the remarkable hexameric assembly of fungal proton pumps, the many ways in which P4-ATPase lipid flippases are regulated, and finally the deorphanization of P5 pumps. Interestingly many of the described features are found in more than one of the five subfamilies, and mixed and matched together to provide optimal function and precise regulation.
KW - P-type ATPases
KW - cryo-EM
KW - activity
KW - regulation
UR - http://www.scopus.com/inward/record.url?scp=85164209456&partnerID=8YFLogxK
U2 - 10.1042/BST20221543
DO - 10.1042/BST20221543
M3 - Review
C2 - 37264943
SN - 0300-5127
VL - 51
SP - 1347
EP - 1360
JO - Biochemical Society Transactions
JF - Biochemical Society Transactions
IS - 3
ER -