The post-translational modification of proteins with lipid moieties confers spatial and temporal control of protein function by restricting their subcellular distribution or movement in the extracellular milieu. Yet, little is known about the significance of lipid selectivity to the activity of proteins targeted for such modifications. Membrane bound O-acyl transferases (MBOATs) are a superfamily of multipass enzymes that transfer fatty acids on to lipid or protein substrates. Three MBOATs constitute a subfamily with secreted signalling molecules for substrates, the Wnt, Hedgehog (Hh) and Ghrelin proteins. Given their important roles in adult tissue homoeostasis, all three molecules and their respective associated acyltransferases provide a framework for interrogating the role of extracellular acylation events in cell-to-cell communication. Here, we discuss how the preference for a fatty acyl donor in the Wnt acyltransferase porcupine (Porcn) and possibly in other protein lipidation enzymes may provide a means for coupling metabolic health at the single cell level to communal cell fate decision-making in complex multicellular organisms.
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April 2015
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Conference Article|
April 07 2015
Fatty acyl donor selectivity in membrane bound O-acyltransferases and communal cell fate decision-making
Rubina Tuladhar;
Rubina Tuladhar
1
*Departments of Cell Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390, U.S.A.
1To whom correspondence should be addressed (emaillawrence.lum@utsouthwestern.edu).
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Lawrence Lum
Lawrence Lum
*Departments of Cell Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390, U.S.A.
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Publisher: Portland Press Ltd
Received:
October 16 2014
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2015 Biochemical Society
2015
Biochem Soc Trans (2015) 43 (2): 235–239.
Article history
Received:
October 16 2014
Citation
Rubina Tuladhar, Lawrence Lum; Fatty acyl donor selectivity in membrane bound O-acyltransferases and communal cell fate decision-making. Biochem Soc Trans 1 April 2015; 43 (2): 235–239. doi: https://doi.org/10.1042/BST20140282
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