气候变化领域集成服务门户(CCPortal): Myristoylation alone is sufficient for PKA catalytic subunits to associate with the plasma membrane to regulate neuronal functions

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DOI	10.1073/pnas.2021658118
	Myristoylation alone is sufficient for PKA catalytic subunits to associate with the plasma membrane to regulate neuronal functions
	Xiong W.-H.; Qin M.; Zhong H.
发表日期	2021
ISSN	00278424
卷号	118 期号:15
英文摘要	Myristoylation is a posttranslational modification that plays diverse functional roles in many protein species. The myristate moiety is considered insufficient for protein-membrane associations unless additional membrane-affinity motifs, such as a stretch of positively charged residues, are present. Here, we report that the electrically neutral N-terminal fragment of the protein kinase A catalytic subunit (PKA-C), in which myristoylation is the only functional motif, is sufficient for membrane association. This myristoylation can associate a fraction of PKA-C molecules or fluorescent proteins (FPs) to the plasma membrane in neuronal dendrites. The net neutral charge of the PKA-C N terminus is evolutionally conserved, even though its membrane affinity can be readily tuned by changing charges near the myristoylation site. The observed membrane association, while moderate, is sufficient to concentrate PKA activity at the membrane by nearly 20-fold and is required for PKA regulation of AMPA receptors at neuronal synapses. Our results indicate that myristoylation may be sufficient to drive functionally significant membrane association in the absence of canonical assisting motifs. This provides a revised conceptual base for the understanding of how myristoylation regulates protein functions. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	CAMP-dependent kinase; Fractional membrane association; Myristoylation; PKA
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/179879
作者单位	Vollum Institute, Oregon Health and Science University, Portland, OR 97239, United States
推荐引用方式 GB/T 7714	Xiong W.-H.,Qin M.,Zhong H.. Myristoylation alone is sufficient for PKA catalytic subunits to associate with the plasma membrane to regulate neuronal functions[J],2021,118(15).
APA	Xiong W.-H.,Qin M.,&Zhong H..(2021).Myristoylation alone is sufficient for PKA catalytic subunits to associate with the plasma membrane to regulate neuronal functions.Proceedings of the National Academy of Sciences of the United States of America,118(15).
MLA	Xiong W.-H.,et al."Myristoylation alone is sufficient for PKA catalytic subunits to associate with the plasma membrane to regulate neuronal functions".Proceedings of the National Academy of Sciences of the United States of America 118.15(2021).