Structure and Mechanism of P-Type ATPase Ion Pumps

Mateusz Dyla; Magnus Kjærgaard; Hanne Poulsen; Poul Nissen

doi:10.1146/annurev-biochem-010611-112801

Structure and Mechanism of P-Type ATPase Ion Pumps

Mateusz Dyla, Magnus Kjærgaard, Hanne Poulsen, Poul Nissen

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

118 Citationer (Scopus)

Abstract

P-type ATPases are found in all kingdoms of life and constitute a wide range of cation transporters, primarily for H ⁺, Na ⁺, K ⁺, Ca ²⁺, and transition metal ions such as Cu(I), Zn(II), and Cd(II). They have been studied through a wide range of techniques, and research has gained very significant insight on their transport mechanism and regulation. Here, we review the structure, function, and dynamics of P2-ATPases including Ca ²⁺-ATPases and Na,K-ATPase. We highlight mechanisms of functional transitions that are associated with ion exchange on either side of the membrane and how the functional cycle is regulated by interaction partners, autoregulatory domains, and off-cycle states. Finally, we discuss future perspectives based on emerging techniques and insights.

Originalsprog	Engelsk
Tidsskrift	Annual Review of Biochemistry
Vol/bind	89
Sider (fra-til)	583-603
Antal sider	21
ISSN	0066-4154
DOI	https://doi.org/10.1146/annurev-biochem-010611-112801
Status	Udgivet - jun. 2020

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10.1146/annurev-biochem-010611-112801

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title = "Structure and Mechanism of P-Type ATPase Ion Pumps",

abstract = "P-type ATPases are found in all kingdoms of life and constitute a wide range of cation transporters, primarily for H +, Na +, K +, Ca 2+, and transition metal ions such as Cu(I), Zn(II), and Cd(II). They have been studied through a wide range of techniques, and research has gained very significant insight on their transport mechanism and regulation. Here, we review the structure, function, and dynamics of P2-ATPases including Ca 2+-ATPases and Na,K-ATPase. We highlight mechanisms of functional transitions that are associated with ion exchange on either side of the membrane and how the functional cycle is regulated by interaction partners, autoregulatory domains, and off-cycle states. Finally, we discuss future perspectives based on emerging techniques and insights. ",

keywords = "Ca -ATPase, Na,K-ATPase, autoinhibition, intrinsically disordered, membrane transport protein, single molecule, 1ST TRANSMEMBRANE HELIX, PROTEIN, K+-ATPASE, CRYSTAL-STRUCTURE, ADENOSINE-TRIPHOSPHATASE, Ca2+-ATPase, PHOSPHOLAMBAN INHIBITION, SKELETAL-MUSCLE, SARCOPLASMIC-RETICULUM CA2+-ATPASE, INTRINSICALLY DISORDERED REGIONS, CALCIUM-PUMP",

author = "Mateusz Dyla and Magnus Kj{\ae}rgaard and Hanne Poulsen and Poul Nissen",

year = "2020",

month = jun,

doi = "10.1146/annurev-biochem-010611-112801",

language = "English",

volume = "89",

pages = "583--603",

journal = "Annual Review of Biochemistry",

issn = "0066-4154",

publisher = "Annual Reviews Inc.",

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TY - JOUR

T1 - Structure and Mechanism of P-Type ATPase Ion Pumps

AU - Dyla, Mateusz

AU - Kjærgaard, Magnus

AU - Poulsen, Hanne

AU - Nissen, Poul

PY - 2020/6

Y1 - 2020/6

N2 - P-type ATPases are found in all kingdoms of life and constitute a wide range of cation transporters, primarily for H +, Na +, K +, Ca 2+, and transition metal ions such as Cu(I), Zn(II), and Cd(II). They have been studied through a wide range of techniques, and research has gained very significant insight on their transport mechanism and regulation. Here, we review the structure, function, and dynamics of P2-ATPases including Ca 2+-ATPases and Na,K-ATPase. We highlight mechanisms of functional transitions that are associated with ion exchange on either side of the membrane and how the functional cycle is regulated by interaction partners, autoregulatory domains, and off-cycle states. Finally, we discuss future perspectives based on emerging techniques and insights.

AB - P-type ATPases are found in all kingdoms of life and constitute a wide range of cation transporters, primarily for H +, Na +, K +, Ca 2+, and transition metal ions such as Cu(I), Zn(II), and Cd(II). They have been studied through a wide range of techniques, and research has gained very significant insight on their transport mechanism and regulation. Here, we review the structure, function, and dynamics of P2-ATPases including Ca 2+-ATPases and Na,K-ATPase. We highlight mechanisms of functional transitions that are associated with ion exchange on either side of the membrane and how the functional cycle is regulated by interaction partners, autoregulatory domains, and off-cycle states. Finally, we discuss future perspectives based on emerging techniques and insights.

KW - Ca -ATPase

KW - Na,K-ATPase

KW - autoinhibition

KW - intrinsically disordered

KW - membrane transport protein

KW - single molecule

KW - 1ST TRANSMEMBRANE HELIX

KW - PROTEIN

KW - K+-ATPASE

KW - CRYSTAL-STRUCTURE

KW - ADENOSINE-TRIPHOSPHATASE

KW - Ca2+-ATPase

KW - PHOSPHOLAMBAN INHIBITION

KW - SKELETAL-MUSCLE

KW - SARCOPLASMIC-RETICULUM CA2+-ATPASE

KW - INTRINSICALLY DISORDERED REGIONS

KW - CALCIUM-PUMP

U2 - 10.1146/annurev-biochem-010611-112801

DO - 10.1146/annurev-biochem-010611-112801

M3 - Journal article

C2 - 31874046

SN - 0066-4154

VL - 89

SP - 583

EP - 603

JO - Annual Review of Biochemistry

JF - Annual Review of Biochemistry

ER -

Structure and Mechanism of P-Type ATPase Ion Pumps

Abstract

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