ArticleThe Journal of biological chemistry2010
Dual anchoring of the GRASP membrane tether promotes trans pairing.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- Protein lipidation in cardiovascular homeostasis, development, and disease.Clinical science (London, England : 1979) · 2026Review
- The Functions of the Golgin Family of Coiled-Coil Proteins.Sub-cellular biochemistry · 2026Review
- A distinct Golgi-targeting mechanism of dGM130 inFrontiers in molecular neuroscience · 2023Article
- Retro-2 alters Golgi structure.Scientific reports · 2022Article
- Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure.The Journal of cell biology · 2021Article
- The Role of GM130 in Nervous System Diseases.Frontiers in neurology · 2021Review
- Nonredundant Roles of GRASP55 and GRASP65 in the Golgi Apparatus and Beyond.Trends in biochemical sciences · 2020Review
- The function of GORASPs in Golgi apparatus organization in vivo.The Journal of cell biology · 2020Article
- Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack.Scientific reports · 2019Article
- The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior.Scientific reports · 2018Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- Structural Basis for the Interaction between Golgi Reassembly-stacking Protein GRASP55 and Golgin45.The Journal of biological chemistry · 2017Article
- Article
- Glycosylation Quality Control by the Golgi Structure.Journal of molecular biology · 2016Review
- Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016Review
- COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex.Scientific reports · 2016Article
- Fatty acylation of proteins: The long and the short of it.Progress in lipid research · 2016Review
- GRASP: A Multitasking Tether.Frontiers in cell and developmental biology · 2016Review
- Mena-GRASP65 interaction couples actin polymerization to Golgi ribbon linking.Molecular biology of the cell · 2016Article
- Structural basis for the interaction between the Golgi reassembly-stacking protein GRASP65 and the Golgi matrix protein GM130.The Journal of biological chemistry · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
GRASP proteins share an N-terminal GRASP domain and mediate homotypic tethering of Golgi cisternae to form extended Golgi ribbons. The golgin GM130 is thought to bind the C-terminal side of the GRASP domain to recruit GRASP65 onto the Golgi whereas stable membrane association appears to also depend on anchoring of the N terminus by myristoylation. Here, we examine the nature of the GM130/GRASP65 interaction and test whether the dual membrane contacts of the GRASP domain have a role in tethering beyond membrane recruitment. GM130 was found to contain a C-terminal PDZ ligand that binds the putative groove of the second PDZ-like domain in GRASP65. To test tethering activity independent of targeting, we took advantage of a tethering assay carried out on the mitochondrial membrane in which the GRASP membrane attachment points were individually or simultaneously substituted with mitochondrially targeted transmembrane sequences. N-terminally anchored constructs tethered only if the C terminus was also anchored; and likewise, C-terminally anchored constructs tethered only if the N terminus was anchored. One explanation for the role of this dual anchoring is that it orients the GRASP domain to prevent cis interactions within the same membrane thereby favoring trans interactions between adjacent membranes. Indeed, singly anchored GRASP constructs, although nonfunctional in tethering, interacted with one another and also bound and inhibited dually anchored constructs. This work thus elucidates the GM130/GRASP65 interaction and supports a novel orientation-based model of membrane tether regulation in which dual membrane contact orients the tethering interaction interface to favor trans over cis interactions.
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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.