Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells.

Jesper S Hansen; Nils J Færgeman; Birthe B Kragelund; Jens Knudsen

doi:10.1042/BJ20070559

Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells.

Jesper S Hansen, Nils J Færgeman, Birthe B Kragelund, Jens Knudsen

Biomolecular Sciences

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

29 Citationer (Scopus)

Abstract

Udgivelsesdato: 2008-Mar-15

Originalsprog	Engelsk
Tidsskrift	Biochemical Journal
Vol/bind	410
Udgave nummer	3
Sider (fra-til)	463-472
Antal sider	9
ISSN	0264-6021
DOI	https://doi.org/10.1042/BJ20070559
Status	Udgivet - 2008

Bibliografisk note

Key words: acyl-CoA-binding protein (ACBP), confocal microscopy, endoplasmic reticulum, Golgi, trafficking, two-photon excitation fluorescence recovery after photobleaching (FRAP).

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Citationsformater

@article{2140ac90e3b311dcbee902004c4f4f50,

title = "Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells.",

abstract = "In the present study, we microinjected fluorescently labelled liver bovine ACBP (acyl-CoA-binding protein) [FACI-50 (fluorescent acyl-CoA indicator-50)] into HeLa and BMGE (bovine mammary gland epithelial) cell lines to characterize the localization and dynamics of ACBP in living cells. Results showed that ACBP targeted to the ER (endoplasmic reticulum) and Golgi in a ligand-binding-dependent manner. A variant Y28F/K32A-FACI-50, which is unable to bind acyl-CoA, did no longer show association with the ER and became segregated from the Golgi, as analysed by intensity correlation calculations. Depletion of fatty acids from cells by addition of FAFBSA (fatty-acid-free BSA) significantly decreased FACI-50 association with the Golgi, whereas fatty acid overloading increased Golgi association, strongly supporting that ACBP associates with the Golgi in a ligand-dependent manner. FRAP (fluorescence recovery after photobleaching) showed that the fatty-acid-induced targeting of FACI-50 to the Golgi resulted in a 5-fold reduction in FACI-50 mobility. We suggest that ACBP is targeted to the ER and Golgi in a ligand-binding-dependent manner in living cells and propose that ACBP may be involved in vesicular trafficking.",

author = "Hansen, {Jesper S} and F{\ae}rgeman, {Nils J} and Kragelund, {Birthe B} and Jens Knudsen",

note = "Key words: acyl-CoA-binding protein (ACBP), confocal microscopy, endoplasmic reticulum, Golgi, trafficking, two-photon excitation fluorescence recovery after photobleaching (FRAP).",

year = "2008",

doi = "10.1042/BJ20070559",

language = "English",

volume = "410",

pages = "463--472",

journal = "Biochemical Journal",

issn = "0264-6021",

publisher = "Portland Press Ltd.",

number = "3",

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TY - JOUR

T1 - Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells.

AU - Hansen, Jesper S

AU - Færgeman, Nils J

AU - Kragelund, Birthe B

AU - Knudsen, Jens

N1 - Key words: acyl-CoA-binding protein (ACBP), confocal microscopy, endoplasmic reticulum, Golgi, trafficking, two-photon excitation fluorescence recovery after photobleaching (FRAP).

PY - 2008

Y1 - 2008

N2 - In the present study, we microinjected fluorescently labelled liver bovine ACBP (acyl-CoA-binding protein) [FACI-50 (fluorescent acyl-CoA indicator-50)] into HeLa and BMGE (bovine mammary gland epithelial) cell lines to characterize the localization and dynamics of ACBP in living cells. Results showed that ACBP targeted to the ER (endoplasmic reticulum) and Golgi in a ligand-binding-dependent manner. A variant Y28F/K32A-FACI-50, which is unable to bind acyl-CoA, did no longer show association with the ER and became segregated from the Golgi, as analysed by intensity correlation calculations. Depletion of fatty acids from cells by addition of FAFBSA (fatty-acid-free BSA) significantly decreased FACI-50 association with the Golgi, whereas fatty acid overloading increased Golgi association, strongly supporting that ACBP associates with the Golgi in a ligand-dependent manner. FRAP (fluorescence recovery after photobleaching) showed that the fatty-acid-induced targeting of FACI-50 to the Golgi resulted in a 5-fold reduction in FACI-50 mobility. We suggest that ACBP is targeted to the ER and Golgi in a ligand-binding-dependent manner in living cells and propose that ACBP may be involved in vesicular trafficking.

AB - In the present study, we microinjected fluorescently labelled liver bovine ACBP (acyl-CoA-binding protein) [FACI-50 (fluorescent acyl-CoA indicator-50)] into HeLa and BMGE (bovine mammary gland epithelial) cell lines to characterize the localization and dynamics of ACBP in living cells. Results showed that ACBP targeted to the ER (endoplasmic reticulum) and Golgi in a ligand-binding-dependent manner. A variant Y28F/K32A-FACI-50, which is unable to bind acyl-CoA, did no longer show association with the ER and became segregated from the Golgi, as analysed by intensity correlation calculations. Depletion of fatty acids from cells by addition of FAFBSA (fatty-acid-free BSA) significantly decreased FACI-50 association with the Golgi, whereas fatty acid overloading increased Golgi association, strongly supporting that ACBP associates with the Golgi in a ligand-dependent manner. FRAP (fluorescence recovery after photobleaching) showed that the fatty-acid-induced targeting of FACI-50 to the Golgi resulted in a 5-fold reduction in FACI-50 mobility. We suggest that ACBP is targeted to the ER and Golgi in a ligand-binding-dependent manner in living cells and propose that ACBP may be involved in vesicular trafficking.

U2 - 10.1042/BJ20070559

DO - 10.1042/BJ20070559

M3 - Journal article

C2 - 17953517

SN - 0264-6021

VL - 410

SP - 463

EP - 472

JO - Biochemical Journal

JF - Biochemical Journal

IS - 3

ER -