ArticlePloS one2013
Protein N-myristoylation plays a critical role in the endoplasmic reticulum morphological change induced by overexpression of protein Lunapark, an integral membrane protein of the endoplasmic reticulum.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 54 citations in OpenAlex.
- Protein lipidation in cardiovascular homeostasis, development, and disease.Clinical science (London, England : 1979) · 2026Review
- Processes and therapeutic perspectives of acylation modifications of lysine and cysteine in tumors.Cell communication and signaling : CCS · 2026Review
- Protein N-myristoylation plays a critical role in the mitochondrial localization of human mitochondrial complex I accessory subunit NDUFB7.Scientific reports · 2023Article
- Structural Diversity within the Endoplasmic Reticulum-From the Microscale to the Nanoscale.Cold Spring Harbor perspectives in biology · 2023Review
- Blockade of NMT1 enzymatic activity inhibits N-myristoylation of VILIP3 protein and suppresses liver cancer progression.Signal transduction and targeted therapy · 2023Article
- Functional Characterization of the Cystine-Rich-Receptor-like Kinases (International journal of molecular sciences · 2022Article
- Identification of mEAK-7 as a human V-ATPase regulator via cryo-EM data mining.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- ANKRD22 is an N-myristoylated hairpin-like monotopic membrane protein specifically localized to lipid droplets.Scientific reports · 2021Article
- Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021Article
- Lem2 and Lnp1 maintain the membrane boundary between the nuclear envelope and endoplasmic reticulum.Communications biology · 2020Article
- Post-translational protein modifications in schizophrenia.NPJ schizophrenia · 2020Review
- CAND1 regulates lunapark for the proper tubular network of the endoplasmic reticulum.Scientific reports · 2019Article
- Inhibition of N-myristoyltransferase1 affects dengue virus replication.MicrobiologyOpen · 2019Article
- Reciprocal regulation between lunapark and atlastin facilitates ER three-way junction formation.Protein & cell · 2019Article
- A strategy to identify protein-N-myristoylation-dependent phosphorylation reactions of cellular proteins by using Phos-tag SDS-PAGE.PloS one · 2019Article
- Mutations in LNPK, Encoding the Endoplasmic Reticulum Junction Stabilizer Lunapark, Cause a Recessive Neurodevelopmental Syndrome.American journal of human genetics · 2018Article
- Arabidopsis Lunapark proteins are involved in ER cisternae formation.The New phytologist · 2018Article
- Mammalian EAK-7 activates alternative mTOR signaling to regulate cell proliferation and migration.Science advances · 2018Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-myristoylation of eukaryotic cellular proteins has been recognized as a modification that occurs mainly on cytoplasmic proteins. In this study, we examined the membrane localization, membrane integration, and intracellular localization of four recently identified human N-myristoylated proteins with predicted transmembrane domains. As a result, it was found that protein Lunapark, the human ortholog of yeast protein Lnp1p that has recently been found to be involved in network formation of the endoplasmic reticulum (ER), is an N-myristoylated polytopic integral membrane protein. Analysis of tumor necrosis factor-fusion proteins with each of the two putative transmembrane domains and their flanking regions of protein Lunapark revealed that transmembrane domain 1 and 2 functioned as type II signal anchor sequence and stop transfer sequence, respectively, and together generated a double-spanning integral membrane protein with an N-/C-terminal cytoplasmic orientation. Immunofluorescence staining of HEK293T cells transfected with a cDNA encoding protein Lunapark tagged with FLAG-tag at its C-terminus revealed that overexpressed protein Lunapark localized mainly to the peripheral ER and induced the formation of large polygonal tubular structures. Morphological changes in the ER induced by overexpressed protein Lunapark were significantly inhibited by the inhibition of protein N-myristoylation by means of replacing Gly2 with Ala. These results indicated that protein N-myristoylation plays a critical role in the ER morphological change induced by overexpression of protein Lunapark.
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