Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA a-subunit

Rosa Laura Lopez Marques; Lisbeth Rosager Poulsen; Susanne Hanisch; Katharina Meffert; Morten Jeppe Buch-Pedersen; Mia Kyed Jakobsen; Thomas Günther-Pomorski; Michael Palmgren

doi:10.1091/mbc.E09-08-0656

Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P₄-ATPase complex reside in the catalytic ALA a-subunit

Rosa Laura Lopez Marques, Lisbeth Rosager Poulsen, Susanne Hanisch, Katharina Meffert, Morten Jeppe Buch-Pedersen, Mia Kyed Jakobsen, Thomas Günther-Pomorski, Michael Palmgren

66 Citationer (Scopus)

Abstract

Members of the P₄ subfamily of P-type ATPases are believed to catalyze flipping of phospholipids across cellular membranes, in this way contributing to vesicle biogenesis in the secretory and endocytic pathways. P₄-ATPases form heteromeric complexes with Cdc50-like proteins, and it has been suggested that these act as β-subunits in the P4-ATPase transport machinery. In this work, we investigated the role of Cdc50-like β-subunits of P₄-ATPases for targeting and function of P ₄-ATPase catalytic β-subunits. We show that the Arabidopsis P₄-ATPases ALA2 and ALA3 gain functionality when coexpressed with any of three different ALIS Cdc50-like β-subunits. However, the final cellular destination of P₄-ATPases as well as their lipid substrate specificity are independent of the nature of the ALIS β-subunit they were allowed to interact with.

Originalsprog	Engelsk
Tidsskrift	Molecular Biology of the Cell
Vol/bind	21
Udgave nummer	5
Sider (fra-til)	791-801
Antal sider	11
ISSN	1059-1524
DOI	https://doi.org/10.1091/mbc.E09-08-0656
Status	Udgivet - 1 mar. 2010

Adgang til dokumentet

10.1091/mbc.E09-08-0656

Citationsformater

Lopez Marques, R. L., Poulsen, L. R., Hanisch, S., Meffert, K., Buch-Pedersen, M. J., Jakobsen, M. K., Günther-Pomorski, T., & Palmgren, M. (2010). Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P₄-ATPase complex reside in the catalytic ALA a-subunit. Molecular Biology of the Cell, 21(5), 791-801. https://doi.org/10.1091/mbc.E09-08-0656

Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P₄-ATPase complex reside in the catalytic ALA a-subunit. / Lopez Marques, Rosa Laura; Poulsen, Lisbeth Rosager; Hanisch, Susanne et al.
I: Molecular Biology of the Cell, Bind 21, Nr. 5, 01.03.2010, s. 791-801.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Lopez Marques, RL, Poulsen, LR, Hanisch, S, Meffert, K, Buch-Pedersen, MJ, Jakobsen, MK, Günther-Pomorski, T & Palmgren, M 2010, 'Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P₄-ATPase complex reside in the catalytic ALA a-subunit', Molecular Biology of the Cell, bind 21, nr. 5, s. 791-801. https://doi.org/10.1091/mbc.E09-08-0656

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title = "Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA a-subunit",

abstract = "Members of the P4 subfamily of P-type ATPases are believed to catalyze flipping of phospholipids across cellular membranes, in this way contributing to vesicle biogenesis in the secretory and endocytic pathways. P4-ATPases form heteromeric complexes with Cdc50-like proteins, and it has been suggested that these act as β-subunits in the P4-ATPase transport machinery. In this work, we investigated the role of Cdc50-like β-subunits of P4-ATPases for targeting and function of P 4-ATPase catalytic β-subunits. We show that the Arabidopsis P4-ATPases ALA2 and ALA3 gain functionality when coexpressed with any of three different ALIS Cdc50-like β-subunits. However, the final cellular destination of P4-ATPases as well as their lipid substrate specificity are independent of the nature of the ALIS β-subunit they were allowed to interact with.",

author = "{Lopez Marques}, {Rosa Laura} and Poulsen, {Lisbeth Rosager} and Susanne Hanisch and Katharina Meffert and Buch-Pedersen, {Morten Jeppe} and Jakobsen, {Mia Kyed} and Thomas G{\"u}nther-Pomorski and Michael Palmgren",

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doi = "10.1091/mbc.E09-08-0656",

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T1 - Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA a-subunit

AU - Lopez Marques, Rosa Laura

AU - Poulsen, Lisbeth Rosager

AU - Hanisch, Susanne

AU - Meffert, Katharina

AU - Buch-Pedersen, Morten Jeppe

AU - Jakobsen, Mia Kyed

AU - Günther-Pomorski, Thomas

AU - Palmgren, Michael

PY - 2010/3/1

Y1 - 2010/3/1

N2 - Members of the P4 subfamily of P-type ATPases are believed to catalyze flipping of phospholipids across cellular membranes, in this way contributing to vesicle biogenesis in the secretory and endocytic pathways. P4-ATPases form heteromeric complexes with Cdc50-like proteins, and it has been suggested that these act as β-subunits in the P4-ATPase transport machinery. In this work, we investigated the role of Cdc50-like β-subunits of P4-ATPases for targeting and function of P 4-ATPase catalytic β-subunits. We show that the Arabidopsis P4-ATPases ALA2 and ALA3 gain functionality when coexpressed with any of three different ALIS Cdc50-like β-subunits. However, the final cellular destination of P4-ATPases as well as their lipid substrate specificity are independent of the nature of the ALIS β-subunit they were allowed to interact with.

AB - Members of the P4 subfamily of P-type ATPases are believed to catalyze flipping of phospholipids across cellular membranes, in this way contributing to vesicle biogenesis in the secretory and endocytic pathways. P4-ATPases form heteromeric complexes with Cdc50-like proteins, and it has been suggested that these act as β-subunits in the P4-ATPase transport machinery. In this work, we investigated the role of Cdc50-like β-subunits of P4-ATPases for targeting and function of P 4-ATPase catalytic β-subunits. We show that the Arabidopsis P4-ATPases ALA2 and ALA3 gain functionality when coexpressed with any of three different ALIS Cdc50-like β-subunits. However, the final cellular destination of P4-ATPases as well as their lipid substrate specificity are independent of the nature of the ALIS β-subunit they were allowed to interact with.

U2 - 10.1091/mbc.E09-08-0656

DO - 10.1091/mbc.E09-08-0656

M3 - Journal article

C2 - 20053675

SN - 1059-1524

VL - 21

SP - 791

EP - 801

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

IS - 5

ER -

Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA a-subunit

Abstract

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Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P₄-ATPase complex reside in the catalytic ALA a-subunit