{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chavan S"],"funding":["Department of Biotechnology, Ministry of Science and Technology, India"],"pagination":["392"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11071952"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["79(7)"],"pubmed_abstract":["Small extracellular vesicle (sEV)-mediated intercellular communication regulates multiple aspects of growth and development in multicellular organisms. However, the mechanism underlying cargo recruitment into sEVs is currently unclear. We show that the key nucleo-cytoplasmic transport (NCT) protein-RanGTPase, in its GTP-bound form (RanGTP), is enriched in sEVs secreted by mammalian cells. This recruitment of RanGTP into sEVs depends on the export receptor CRM1 (also called XPO1). The recruitment of GAPDH, a candidate cargo protein, into sEVs is regulated by the RanGTP-CRM1axis in a nuclear export signal (NES)-dependent manner. Perturbation of NCT through overexpression or depletion of nuclear transport components affected the recruitment of Ran, CRM1 and GAPDH into sEVs. Our studies, thus,"],"journal":["Cellular and molecular life sciences : CMLS"],"pubmed_title":["RanGTPase links nucleo-cytoplasmic transport to the recruitment of cargoes into small extracellular vesicles."],"pmcid":["PMC11071952"],"funding_grant_id":["BT/PR32331/BRB/10/1774/2019"],"pubmed_authors":["Rapole S","Joseph J","Chavan S","Lonare A","Bellare J","Khuperkar D","Seshadri V","Panigrahi S"],"additional_accession":[]},"is_claimable":false,"name":"RanGTPase links nucleo-cytoplasmic transport to the recruitment of cargoes into small extracellular vesicles.","description":"Small extracellular vesicle (sEV)-mediated intercellular communication regulates multiple aspects of growth and development in multicellular organisms. However, the mechanism underlying cargo recruitment into sEVs is currently unclear. We show that the key nucleo-cytoplasmic transport (NCT) protein-RanGTPase, in its GTP-bound form (RanGTP), is enriched in sEVs secreted by mammalian cells. This recruitment of RanGTP into sEVs depends on the export receptor CRM1 (also called XPO1). The recruitment of GAPDH, a candidate cargo protein, into sEVs is regulated by the RanGTP-CRM1axis in a nuclear export signal (NES)-dependent manner. Perturbation of NCT through overexpression or depletion of nuclear transport components affected the recruitment of Ran, CRM1 and GAPDH into sEVs. Our studies, thus,","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jul","modification":"2026-06-01T18:48:36.831Z","creation":"2026-05-19T03:07:08.55Z"},"accession":"S-EPMC11071952","cross_references":{"pubmed":["35779171"],"doi":["10.1007/s00018-022-04422-y"]}}