ArticleScientific reports2018
The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 31 citations in OpenAlex.
- The role of N-terminal acetylation on biomolecular condensation.Communications chemistry · 2026Article
- Dendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules.Cell reports · 2025Article
- The potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion.Protein science : a publication of the Protein Society · 2024Article
- Effects of freezing rate on structural changes in L-lactate dehydrogenase during the freezing process.Scientific reports · 2021Article
- Nucleation-dependent amyloid fibrillation of human GRASP55 in aqueous solution.European biophysics journal : EBJ · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
GRASPs are proteins involved in cell processes that seem paradoxical: responsible for shaping the Golgi cisternae and involved in unconventional secretion mechanisms that bypass the Golgi. Despite its physiological relevance, there is still a considerable lack of studies on full-length GRASPs. Our group has previously reported an unexpected behavior of the full-length GRASP from the fungus C. neoformans: its intrinsically-disordered characteristic. Here, we generalize this finding by showing that it is also observed in the GRASP from S. cerevisae (Grh1), which strongly suggests it might be a general property within the GRASP family. Furthermore, Grh1 is also able to form amyloid-like fibrils either upon heating or when submitted to changes in the dielectric constant of its surroundings, a condition that is experienced by the protein when in close contact with membranes of cell compartments, such as the Golgi apparatus. Intrinsic disorder and fibril formation can thus be two structural properties exploited by GRASP during its functional cycle.
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