Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA.

Nils J Faergeman; Majken Wadum; Søren Feddersen; Mark Burton; Birthe B Kragelund; Jens Knudsen

doi:10.1007/s11010-005-9040-3

Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA.

Nils J Faergeman, Majken Wadum, Søren Feddersen, Mark Burton, Birthe B Kragelund, Jens Knudsen

Biomolecular Sciences

62 Citations (Scopus)

Abstract

Besides serving as essential substrates for beta-oxidation and synthesis of triacylglycerols and more complex lipids like sphingolipids and sterol esters, long-chain fatty acyl-CoA esters are increasingly being recognized as important regulators of enzyme activities and gene transcription. Acyl-CoA binding protein, ACBP, has been proposed to play a pivotal role in the intracellular trafficking and utilization of long-chain fatty acyl-CoA esters. Depletion of acyl-CoA binding protein in yeast results in aberrant organelle morphology incl. fragmented vacuoles, multi-layered plasma membranes and accumulation of vesicles of variable sizes. In contrast to synthesis and turn-over of glycerolipids, the levels of very-long-chain fatty acids, long-chain bases and ceramide are severely affected by Acb1p depletion, suggesting that Acb1p, rather than playing a general role, serves specific roles in cellular lipid metabolism.
Udgivelsesdato: 2007-May

Original language	English
Journal	Molecular and Cellular Biochemistry
Volume	299
Issue number	1-2
Pages (from-to)	55-65
Number of pages	10
ISSN	0300-8177
DOIs	https://doi.org/10.1007/s11010-005-9040-3
Publication status	Published - 2007

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10.1007/s11010-005-9040-3

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@article{67ac52b0e3b311dcbee902004c4f4f50,

title = "Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA.",

abstract = "Besides serving as essential substrates for beta-oxidation and synthesis of triacylglycerols and more complex lipids like sphingolipids and sterol esters, long-chain fatty acyl-CoA esters are increasingly being recognized as important regulators of enzyme activities and gene transcription. Acyl-CoA binding protein, ACBP, has been proposed to play a pivotal role in the intracellular trafficking and utilization of long-chain fatty acyl-CoA esters. Depletion of acyl-CoA binding protein in yeast results in aberrant organelle morphology incl. fragmented vacuoles, multi-layered plasma membranes and accumulation of vesicles of variable sizes. In contrast to synthesis and turn-over of glycerolipids, the levels of very-long-chain fatty acids, long-chain bases and ceramide are severely affected by Acb1p depletion, suggesting that Acb1p, rather than playing a general role, serves specific roles in cellular lipid metabolism. Udgivelsesdato: 2007-May",

author = "Faergeman, {Nils J} and Majken Wadum and S{\o}ren Feddersen and Mark Burton and Kragelund, {Birthe B} and Jens Knudsen",

note = "Keywords: Animals; Diazepam Binding Inhibitor; Humans; Phylogeny; Structure-Activity Relationship",

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T1 - Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA.

AU - Faergeman, Nils J

AU - Wadum, Majken

AU - Feddersen, Søren

AU - Burton, Mark

AU - Kragelund, Birthe B

AU - Knudsen, Jens

N1 - Keywords: Animals; Diazepam Binding Inhibitor; Humans; Phylogeny; Structure-Activity Relationship

PY - 2007

Y1 - 2007

N2 - Besides serving as essential substrates for beta-oxidation and synthesis of triacylglycerols and more complex lipids like sphingolipids and sterol esters, long-chain fatty acyl-CoA esters are increasingly being recognized as important regulators of enzyme activities and gene transcription. Acyl-CoA binding protein, ACBP, has been proposed to play a pivotal role in the intracellular trafficking and utilization of long-chain fatty acyl-CoA esters. Depletion of acyl-CoA binding protein in yeast results in aberrant organelle morphology incl. fragmented vacuoles, multi-layered plasma membranes and accumulation of vesicles of variable sizes. In contrast to synthesis and turn-over of glycerolipids, the levels of very-long-chain fatty acids, long-chain bases and ceramide are severely affected by Acb1p depletion, suggesting that Acb1p, rather than playing a general role, serves specific roles in cellular lipid metabolism. Udgivelsesdato: 2007-May

AB - Besides serving as essential substrates for beta-oxidation and synthesis of triacylglycerols and more complex lipids like sphingolipids and sterol esters, long-chain fatty acyl-CoA esters are increasingly being recognized as important regulators of enzyme activities and gene transcription. Acyl-CoA binding protein, ACBP, has been proposed to play a pivotal role in the intracellular trafficking and utilization of long-chain fatty acyl-CoA esters. Depletion of acyl-CoA binding protein in yeast results in aberrant organelle morphology incl. fragmented vacuoles, multi-layered plasma membranes and accumulation of vesicles of variable sizes. In contrast to synthesis and turn-over of glycerolipids, the levels of very-long-chain fatty acids, long-chain bases and ceramide are severely affected by Acb1p depletion, suggesting that Acb1p, rather than playing a general role, serves specific roles in cellular lipid metabolism. Udgivelsesdato: 2007-May

U2 - 10.1007/s11010-005-9040-3

DO - 10.1007/s11010-005-9040-3

M3 - Journal article

C2 - 17013545

SN - 0300-8177

VL - 299

SP - 55

EP - 65

JO - Molecular and Cellular Biochemistry

JF - Molecular and Cellular Biochemistry

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ER -