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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/2680a250e1e54ba7aecb1d6f4993fea7
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Sumario: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.