Covalent attachment of a variety of lipid groups to proteins is now recognized as a major group of post-translational modifications. S-acylation of proteins at cysteine residues is the only modification considered dynamic and thus has the potential for regulating protein function and/or localization. The activities that catalyse reversible S-acylation have not been well characterized and it is not clear whether both the acylation and the deacylation steps are regulated, since in principle it would be sufficient to control only one of them. Both apparently enzymatic and non-enzymatic S-acylation of proteins have previously been reported. Here we show that a synthetic myristoylated c-Yes protein tyrosine kinase undecapeptide undergoes spontaneous S-acylation in vitro when using a long chain acyl-CoA as acyl donor in the absence of any protein. The S-acylation was dependent on myristoylation of the substrate, the length of the incubation period, temperature and substrate concentration. When COS cell fractions were added to the S-acylation reaction no additional peptide:S-acyltransferase activity was detected. These results are consistent with the possibility that membrane-associated proteins may undergo S-acylation in vivo by non-enzymatic transfer of acyl groups from acyl-CoA. In this case, the S-acylation-deacylation process could be controlled by a regulated depalmitoylation mechanism.
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March 1998
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Research Article|
March 01 1998
Pseudo-enzymatic S-acylation of a myristoylated Yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo Available to Purchase
M. Carmen BAÑÓ;
M. Carmen BAÑÓ
1
1Division of Membrane Biology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, U.K.
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S. Caroline JACKSON;
S. Caroline JACKSON
1Division of Membrane Biology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, U.K.
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I. Anthony MAGEE
I. Anthony MAGEE
2
1Division of Membrane Biology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, U.K.
2To whom correspondence should be addressed.
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Publisher: Portland Press Ltd
Received:
June 16 1997
Revision Received:
October 29 1997
Accepted:
November 06 1997
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1998
1998
Biochem J (1998) 330 (2): 723–731.
Article history
Received:
June 16 1997
Revision Received:
October 29 1997
Accepted:
November 06 1997
Citation
M. Carmen BAÑÓ, S. Caroline JACKSON, I. Anthony MAGEE; Pseudo-enzymatic S-acylation of a myristoylated Yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo. Biochem J 1 March 1998; 330 (2): 723–731. doi: https://doi.org/10.1042/bj3300723
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