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

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A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein. / Ekberg, Kira; Palmgren, Michael; Veierskov, Bjarke; Buch-Pedersen, Morten Jeppe.

I: Journal of Biological Chemistry, Bind 285, Nr. 10, 2010, s. 7344-7350.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Ekberg, K, Palmgren, M, Veierskov, B & Buch-Pedersen, MJ 2010, 'A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein', Journal of Biological Chemistry, bind 285, nr. 10, s. 7344-7350. https://doi.org/10.1074/jbc.M109.096123

APA

Ekberg, K., Palmgren, M., Veierskov, B., & Buch-Pedersen, M. J. (2010). A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein. Journal of Biological Chemistry, 285(10), 7344-7350. https://doi.org/10.1074/jbc.M109.096123

Vancouver

Ekberg K, Palmgren M, Veierskov B, Buch-Pedersen MJ. A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein. Journal of Biological Chemistry. 2010;285(10):7344-7350. https://doi.org/10.1074/jbc.M109.096123

Author

Ekberg, Kira ; Palmgren, Michael ; Veierskov, Bjarke ; Buch-Pedersen, Morten Jeppe. / A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein. I: Journal of Biological Chemistry. 2010 ; Bind 285, Nr. 10. s. 7344-7350.

Bibtex

@article{2af675c0e01e11dfb6d2000ea68e967b,
title = "A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein",
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. ",
author = "Kira Ekberg and Michael Palmgren and Bjarke Veierskov and Buch-Pedersen, {Morten Jeppe}",
year = "2010",
doi = "10.1074/jbc.M109.096123",
language = "English",
volume = "285",
pages = "7344--7350",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "10",

}

RIS

TY - JOUR

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

PY - 2010

Y1 - 2010

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.

U2 - 10.1074/jbc.M109.096123

DO - 10.1074/jbc.M109.096123

M3 - Journal article

VL - 285

SP - 7344

EP - 7350

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 10

ER -

ID: 22705375