ArticleSmall GTPases
High yield production of myristoylated Arf6 small GTPase by recombinant N-myristoyl transferase.
Article in Small GTPases. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Binding with heat shock cognate protein HSC70 fine-tunes the Golgi association of the small GTPase ARL5B.The Journal of biological chemistry · 2021Article
- Article
- In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Ciliary Machinery Is Repurposed for T Cell Immune Synapse Trafficking of LCK.Developmental cell · 2018Article
- Article
- EFA6 controls Arf1 and Arf6 activation through a negative feedback loop.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Integrated conformational and lipid-sensing regulation of endosomal ArfGEF BRAG2.PLoS biology · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small GTP-binding proteins of the Arf family (Arf GTPases) interact with multiple cellular partners and with membranes to regulate intracellular traffic and organelle structure. Understanding the underlying molecular mechanisms requires in vitro biochemical assays to test for regulations and functions. Such assays should use proteins in their cellular form, which carry a myristoyl lipid attached in N-terminus. N-myristoylation of recombinant Arf GTPases can be achieved by co-expression in E. coli with a eukaryotic N-myristoyl transferase. However, purifying myristoylated Arf GTPases is difficult and has a poor overall yield. Here we show that human Arf6 can be N-myristoylated in vitro by recombinant N-myristoyl transferases from different eukaryotic species. The catalytic efficiency depended strongly on the guanine nucleotide state and was highest for Arf6-GTP. Large-scale production of highly pure N-myristoylated Arf6 could be achieved, which was fully functional for liposome-binding and EFA6-stimulated nucleotide exchange assays. This establishes in vitro myristoylation as a novel and simple method that could be used to produce other myristoylated Arf and Arf-like GTPases for biochemical assays.
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