A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein

Kira Ekberg; Michael Palmgren; Bjarke Veierskov; Morten Jeppe Buch-Pedersen

doi:10.1074/jbc.M109.096123

A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein

Kira Ekberg, Michael Palmgren, Bjarke Veierskov, Morten Jeppe Buch-Pedersen

42 Citationer (Scopus)

Abstract

The activity of many P-type ATPases is found to be regulated by interacting proteins or autoinhibitory elements located in N- or C-terminal extensions. An extended C terminus of fungal and plant P-type plasma membrane H⁺-ATPases has long been recognized to be part of a regulatory apparatus involving an autoinhibitory domain. Here we demonstrate that both the N and the C termini of the plant plasma membrane H⁺-ATPase are directly involved in controlling the pump activity state and that N-terminal displacements are coupled to secondary modifications taking place at the C-terminal end. This identifies the first group of P-type ATPases for which both ends of the polypeptide chain constitute regulatory domains, which together contribute to the autoinhibitory apparatus. This suggests an intricate mechanism of cis-regulation with both termini of the protein communicating to obtain the necessary control of the enzyme activity state.

Originalsprog	Engelsk
Tidsskrift	Journal of Biological Chemistry
Vol/bind	285
Udgave nummer	10
Sider (fra-til)	7344-7350
Antal sider	7
ISSN	0021-9258
DOI	https://doi.org/10.1074/jbc.M109.096123
Status	Udgivet - 5 mar. 2010

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10.1074/jbc.M109.096123

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abstract = "The activity of many P-type ATPases is found to be regulated by interacting proteins or autoinhibitory elements located in N- or C-terminal extensions. An extended C terminus of fungal and plant P-type plasma membrane H+-ATPases has long been recognized to be part of a regulatory apparatus involving an autoinhibitory domain. Here we demonstrate that both the N and the C termini of the plant plasma membrane H+-ATPase are directly involved in controlling the pump activity state and that N-terminal displacements are coupled to secondary modifications taking place at the C-terminal end. This identifies the first group of P-type ATPases for which both ends of the polypeptide chain constitute regulatory domains, which together contribute to the autoinhibitory apparatus. This suggests an intricate mechanism of cis-regulation with both termini of the protein communicating to obtain the necessary control of the enzyme activity state. ",

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T1 - A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein

AU - Ekberg, Kira

AU - Palmgren, Michael

AU - Veierskov, Bjarke

AU - Buch-Pedersen, Morten Jeppe

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N2 - The activity of many P-type ATPases is found to be regulated by interacting proteins or autoinhibitory elements located in N- or C-terminal extensions. An extended C terminus of fungal and plant P-type plasma membrane H+-ATPases has long been recognized to be part of a regulatory apparatus involving an autoinhibitory domain. Here we demonstrate that both the N and the C termini of the plant plasma membrane H+-ATPase are directly involved in controlling the pump activity state and that N-terminal displacements are coupled to secondary modifications taking place at the C-terminal end. This identifies the first group of P-type ATPases for which both ends of the polypeptide chain constitute regulatory domains, which together contribute to the autoinhibitory apparatus. This suggests an intricate mechanism of cis-regulation with both termini of the protein communicating to obtain the necessary control of the enzyme activity state.

AB - The activity of many P-type ATPases is found to be regulated by interacting proteins or autoinhibitory elements located in N- or C-terminal extensions. An extended C terminus of fungal and plant P-type plasma membrane H+-ATPases has long been recognized to be part of a regulatory apparatus involving an autoinhibitory domain. Here we demonstrate that both the N and the C termini of the plant plasma membrane H+-ATPase are directly involved in controlling the pump activity state and that N-terminal displacements are coupled to secondary modifications taking place at the C-terminal end. This identifies the first group of P-type ATPases for which both ends of the polypeptide chain constitute regulatory domains, which together contribute to the autoinhibitory apparatus. This suggests an intricate mechanism of cis-regulation with both termini of the protein communicating to obtain the necessary control of the enzyme activity state.

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DO - 10.1074/jbc.M109.096123

M3 - Journal article

SN - 0021-9258

VL - 285

SP - 7344

EP - 7350

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

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ER -

A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein

Abstract

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