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 Citations (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.

Original language	English
Journal	Molecular Biology of the Cell
Volume	21
Issue number	5
Pages (from-to)	791-801
Number of pages	11
ISSN	1059-1524
DOIs	https://doi.org/10.1091/mbc.E09-08-0656
Publication status	Published - 1 Mar 2010

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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.
In: Molecular Biology of the Cell, Vol. 21, No. 5, 01.03.2010, p. 791-801.

Research output: Contribution to journal › Journal article › Research › 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, vol. 21, no. 5, pp. 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.",

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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

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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

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SN - 1059-1524

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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