ArticleThe Journal of biological chemistry2014
Myristoylation restricts orientation of the GRASP domain on membranes and promotes membrane tethering.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- Protein lipidation in cardiovascular homeostasis, development, and disease.Clinical science (London, England : 1979) · 2026Review
- Protein lipidation in the tumor microenvironment: enzymology, signaling pathways, and therapeutics.Molecular cancer · 2025Review
- Rab-mediated trafficking in the secondary cells of Drosophila male accessory glands and its role in fecundity.Traffic (Copenhagen, Denmark) · 2019Article
- Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019Review
- New Insights Into the Golgi Stacking Proteins.Frontiers in cell and developmental biology · 2019Review
- The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior.Scientific reports · 2018Article
- Insertion of Dengue E into lipid bilayers studied by neutron reflectivity and molecular dynamics simulations.Biochimica et biophysica acta. Biomembranes · 2018Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- Structural characterization of membrane-bound human immunodeficiency virus-1 Gag matrix with neutron reflectometry.Biointerphases · 2017Article
- Mouse Stbd1 isJournal of cell science · 2017Article
- Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers.The journal of physical chemistry letters · 2017Article
- New structural insights into Golgi Reassembly and Stacking Protein (GRASP) in solution.Scientific reports · 2016Article
- Membrane Binding of HIV-1 Matrix Protein: Dependence on Bilayer Composition and Protein Lipidation.Journal of virology · 2016Article
- GRASP: A Multitasking Tether.Frontiers in cell and developmental biology · 2016Review
- Membrane association of the PTEN tumor suppressor: neutron scattering and MD simulations reveal the structure of protein-membrane complexes.Methods (San Diego, Calif.) · 2015Review
- On the function and homeostasis of PCSK9: reciprocal interaction with LDLR and additional lipid effects.Atherosclerosis · 2015Review
- Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy.The Journal of biological chemistry · 2015Article
- Zooming in on disordered systems: neutron reflection studies of proteins associated with fluid membranes.Biochimica et biophysica acta · 2014Review
- Golgi compartmentation and identity.Current opinion in cell biology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The mammalian Golgi reassembly stacking protein (GRASP) proteins are Golgi-localized homotypic membrane tethers that organize Golgi stacks into a long, contiguous ribbon-like structure. It is unknown how GRASPs undergo trans pairing given that cis interactions between the proteins in the plane of the membrane are intrinsically favored. To test the hypothesis that myristoylation of the self-interacting GRASP domain restricts its orientation on the membrane to favor trans pairing, we established an in vitro assay that recapitulates GRASP-dependent membrane tethering and used neutron reflection under similar conditions to determine the orientation of the GRASP domain. In vivo, the membrane association of GRASP proteins is conferred by the simultaneous insertion of an N-terminal myristic acid and binding to a Golgi-associated binding partner. In our assay, the latter contact was replaced using a C-terminal hexa-His moiety, which bound to Ni(2+)-conjugated lipids incorporated into a substrate-supported bilayer lipid membrane. Nonmyristoylated protein lacked a fixed orientation on the membrane and inefficiently tethered liposomes. In contrast, myristoylated GRASP promoted tethering and exhibited a unique membrane complex. Thus, myristoylation restricts the membrane orientation of the GRASP domain favoring interactions in trans for membrane tethering.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.