biostudies-literatureMendes LFSFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e TecnológicoCoordenação de Aperfeiçoamento de Pessoal de Nível SuperiorFundação de Amparo à Pesquisa do Estado de São PauloCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)e5085https://www.ebi.ac.uk/biostudies/studies/S-EPMC11201811biostudies-literatureUnknown33(7)Eukaryotic cells have developed intricate mechanisms for biomolecule transport, particularly in stressful conditions. This interdisciplinary study delves into unconventional protein secretion (UPS) pathways activated during starvation, facilitating the export of proteins bypassing most of the components of the classical secretory machinery. Specifically, we focus on the underexplored mechanisms of the GRASP's role in UPS, particularly in biogenesis and cargo recruitment for the vesicular-like compartment for UPS. Our results show that liquid-liquid phase separation (LLPS) plays a key role in the coacervation of Grh1, the GRASP yeast homologue, under starvation-like conditions. This association seems a precursor to the Compartment for Unconventional Protein Secretion (CUPS) biogenesis. Grh1Protein science : a publication of the Protein SocietyThe potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion.PMC112018112021/10465-72015/50366‐72020/15542‐72021/10465‐72015/50366-72020/15542-72022/06006-0306682/2018-42009/54044-32022/06006‐02009/54044‐3306682/2018‐4Mendes LFSRout SKGimenes CORiek Rda Silva MDOCosta-Filho AJfalseThe potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion.Eukaryotic cells have developed intricate mechanisms for biomolecule transport, particularly in stressful conditions. This interdisciplinary study delves into unconventional protein secretion (UPS) pathways activated during starvation, facilitating the export of proteins bypassing most of the components of the classical secretory machinery. Specifically, we focus on the underexplored mechanisms of the GRASP's role in UPS, particularly in biogenesis and cargo recruitment for the vesicular-like compartment for UPS. Our results show that liquid-liquid phase separation (LLPS) plays a key role in the coacervation of Grh1, the GRASP yeast homologue, under starvation-like conditions. This association seems a precursor to the Compartment for Unconventional Protein Secretion (CUPS) biogenesis. Grh12024-01-01T00:00:00Z2024 Jul2026-06-01T15:30:09.636Z2026-04-08T13:39:40.801ZS-EPMC112018113892319910.1002/pro.5085