NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle
Lysine fatty acylation is an important protein posttranslational modification but mammalian lysine fatty acyl transferases have remained unknown so far. Here the authors report that the human N-terminal glycine myristoyltransferases 1 and 2 catalyze the addition of myristoyl chains to specific lysin...
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Nature Portfolio
2020
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oai:doaj.org-article:2680a250e1e54ba7aecb1d6f4993fea72021-12-02T15:34:13ZNMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle10.1038/s41467-020-14893-x2041-1723https://doaj.org/article/2680a250e1e54ba7aecb1d6f4993fea72020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14893-xhttps://doaj.org/toc/2041-1723Lysine fatty acylation is an important protein posttranslational modification but mammalian lysine fatty acyl transferases have remained unknown so far. Here the authors report that the human N-terminal glycine myristoyltransferases 1 and 2 catalyze the addition of myristoyl chains to specific lysine residues and show that they myristoylate ARF6 lysine 3, which explains the unusual membrane binding properties of ARF6.Tatsiana KosciukIan R. PriceXiaoyu ZhangChengliang ZhuKayla N. JohnsonShuai ZhangSteve L. HalabyGarrison P. KomanieckiMin YangCaroline J. DeHartPaul M. ThomasNeil L. KelleherJ. Christopher FrommeHening LinNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-17 (2020) |
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Science Q Tatsiana Kosciuk Ian R. Price Xiaoyu Zhang Chengliang Zhu Kayla N. Johnson Shuai Zhang Steve L. Halaby Garrison P. Komaniecki Min Yang Caroline J. DeHart Paul M. Thomas Neil L. Kelleher J. Christopher Fromme Hening Lin NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle |
description |
Lysine fatty acylation is an important protein posttranslational modification but mammalian lysine fatty acyl transferases have remained unknown so far. Here the authors report that the human N-terminal glycine myristoyltransferases 1 and 2 catalyze the addition of myristoyl chains to specific lysine residues and show that they myristoylate ARF6 lysine 3, which explains the unusual membrane binding properties of ARF6. |
format |
article |
author |
Tatsiana Kosciuk Ian R. Price Xiaoyu Zhang Chengliang Zhu Kayla N. Johnson Shuai Zhang Steve L. Halaby Garrison P. Komaniecki Min Yang Caroline J. DeHart Paul M. Thomas Neil L. Kelleher J. Christopher Fromme Hening Lin |
author_facet |
Tatsiana Kosciuk Ian R. Price Xiaoyu Zhang Chengliang Zhu Kayla N. Johnson Shuai Zhang Steve L. Halaby Garrison P. Komaniecki Min Yang Caroline J. DeHart Paul M. Thomas Neil L. Kelleher J. Christopher Fromme Hening Lin |
author_sort |
Tatsiana Kosciuk |
title |
NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle |
title_short |
NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle |
title_full |
NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle |
title_fullStr |
NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle |
title_full_unstemmed |
NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle |
title_sort |
nmt1 and nmt2 are lysine myristoyltransferases regulating the arf6 gtpase cycle |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/2680a250e1e54ba7aecb1d6f4993fea7 |
work_keys_str_mv |
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