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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Autores principales: 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
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/2680a250e1e54ba7aecb1d6f4993fea7
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spelling 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)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle 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
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