Biochemical and cellular functions of P4 ATPases

Lieke M. van der Velden; Stan F. J. van de Graaf; Leo W. J. Klomp

doi:https://doi.org/10.1042/BJ20100644

Biochemical and cellular functions of P4 ATPases

Lieke M. van der Velden, Stan F. J. van de Graaf, Leo W. J. Klomp

Tytgat Institute for Liver and Intestinal Research (AMC)

Research output: Contribution to journal › Review article › Academic › peer-review

16 Citations (Scopus)

Abstract

P4 ATPases (subfamily IV P-type ATPases) form a specialized subfamily of P-type ATPases and have been implicated in phospholipid translocation from the exoplasmic to the cytoplasmic leaflet of biological membranes. Pivotal roles of P4 ATPases have been demonstrated in eukaryotes, ranging from yeast, fungi and plants to mice and humans. P4 ATPases might exert their cellular functions by combining enzymatic phospholipid translocation activity with an enzyme-independent action. The latter could be involved in the timely recruitment of proteins involved in cellular signalling, vesicle coat assembly and cytoskeleton regulation. In the present review, we outline the current knowledge of the biochemical and cellular functions of P4 ATPases in the eukaryotic membrane

Original language	English
Pages (from-to)	1-11
Journal	Biochemical journal
Volume	431
Issue number	1
DOIs	https://doi.org/10.1042/BJ20100644
Publication status	Published - 2010

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https://doi.org/10.1042/BJ20100644

Cite this

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title = "Biochemical and cellular functions of P4 ATPases",

abstract = "P4 ATPases (subfamily IV P-type ATPases) form a specialized subfamily of P-type ATPases and have been implicated in phospholipid translocation from the exoplasmic to the cytoplasmic leaflet of biological membranes. Pivotal roles of P4 ATPases have been demonstrated in eukaryotes, ranging from yeast, fungi and plants to mice and humans. P4 ATPases might exert their cellular functions by combining enzymatic phospholipid translocation activity with an enzyme-independent action. The latter could be involved in the timely recruitment of proteins involved in cellular signalling, vesicle coat assembly and cytoskeleton regulation. In the present review, we outline the current knowledge of the biochemical and cellular functions of P4 ATPases in the eukaryotic membrane",

author = "{van der Velden}, {Lieke M.} and {van de Graaf}, {Stan F. J.} and Klomp, {Leo W. J.}",

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T1 - Biochemical and cellular functions of P4 ATPases

AU - van der Velden, Lieke M.

AU - van de Graaf, Stan F. J.

AU - Klomp, Leo W. J.

PY - 2010

Y1 - 2010

N2 - P4 ATPases (subfamily IV P-type ATPases) form a specialized subfamily of P-type ATPases and have been implicated in phospholipid translocation from the exoplasmic to the cytoplasmic leaflet of biological membranes. Pivotal roles of P4 ATPases have been demonstrated in eukaryotes, ranging from yeast, fungi and plants to mice and humans. P4 ATPases might exert their cellular functions by combining enzymatic phospholipid translocation activity with an enzyme-independent action. The latter could be involved in the timely recruitment of proteins involved in cellular signalling, vesicle coat assembly and cytoskeleton regulation. In the present review, we outline the current knowledge of the biochemical and cellular functions of P4 ATPases in the eukaryotic membrane

AB - P4 ATPases (subfamily IV P-type ATPases) form a specialized subfamily of P-type ATPases and have been implicated in phospholipid translocation from the exoplasmic to the cytoplasmic leaflet of biological membranes. Pivotal roles of P4 ATPases have been demonstrated in eukaryotes, ranging from yeast, fungi and plants to mice and humans. P4 ATPases might exert their cellular functions by combining enzymatic phospholipid translocation activity with an enzyme-independent action. The latter could be involved in the timely recruitment of proteins involved in cellular signalling, vesicle coat assembly and cytoskeleton regulation. In the present review, we outline the current knowledge of the biochemical and cellular functions of P4 ATPases in the eukaryotic membrane

U2 - https://doi.org/10.1042/BJ20100644

DO - https://doi.org/10.1042/BJ20100644

M3 - Review article

C2 - 20836764

SN - 0264-6021

VL - 431

SP - 1

EP - 11

JO - Biochemical journal

JF - Biochemical journal

IS - 1

ER -