{"doi":"10.3390/cells7110198","title":"The Roles of Endo-Lysosomes in Unconventional Protein Secretion","abstract":"<jats:p>Protein secretion in general depends on signal sequence (also named leader sequence), a hydrophobic segment located at or close to the NH2-terminus of a secretory or membrane protein. This sequence guides the entry of nascent polypeptides into the lumen or membranes of the endoplasmic reticulum (ER) for folding, assembly, and export. However, evidence accumulated in recent years has suggested the existence of a collection of unconventional protein secretion (UPS) mechanisms that are independent of the canonical vesicular trafficking route between the ER and the plasma membrane (PM). These UPS mechanisms export soluble proteins bearing no signal sequence. The list of UPS cargos is rapidly expanding, along with the implicated biological functions, but molecular mechanisms accountable for the secretion of leaderless proteins are still poorly defined. This review summarizes our current understanding of UPS mechanisms with an emphasis on the emerging role of endo-lysosomes in this process.</jats:p>","journal":"Cells","year":2018,"id":23992,"datarank":1.0448953602531077,"base_score":3.4339872044851463,"endowment":3.4339872044851463,"self_citation_contribution":0.515098080672772,"citation_network_contribution":0.5297972795803357,"self_endowment_contribution":0.515098080672772,"citer_contribution":0.5297972795803357,"corpus_percentile":null,"corpus_rank":null,"citation_count":30,"citer_count":26,"citers_with_citation_signal":25,"citers_with_endowment":25,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":145321,"name":"Yihong Ye","orcid":null,"position":1,"is_corresponding":false},{"id":145319,"name":"Juhyung Lee","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":3.4339872044851463,"endowment":3.4339872044851463,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"30400277","pmcid":"PMC6262434","openalex_id":"https://openalex.org/W2898878467","authors":[],"funders":[{"funder_name":"National Institute of Diabetes and Digestive and Kidney Diseases","grant_id":"DK075145-02","title":null}],"total_grants":1,"fwci":2.1168,"citation_percentile":0.8661229,"influential_citations":1,"citation_trend":[{"year":2019,"count":3},{"year":2020,"count":9},{"year":2021,"count":6},{"year":2022,"count":7},{"year":2024,"count":3},{"year":2025,"count":2}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://www.mdpi.com/2073-4409/7/11/198/pdf?version=1541223316","host_type":"journal"},{"url":"https://www.mdpi.com/2073-4409/7/11/198/pdf?version=1541223316","host_type":"GOLD"},{"url":"https://www.mdpi.com/2073-4409/7/11/198/pdf?version=1541223316","host_type":"publisher"},{"url":"https://www.mdpi.com/2073-4409/7/11/198/pdf","host_type":"publisher"},{"url":"https://doi.org/10.3390/cells7110198","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/30400277","host_type":"repository"},{"url":"https://doaj.org/article/156d1a8240e64bca910abf0739b29abe","host_type":"repository"},{"url":"http://europepmc.org/pmc/articles/PMC6262434","host_type":"repository"},{"url":"http://dx.doi.org/10.3390/cells7110198","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6262434","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC6262434","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC6262434?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Cellular transport and secretion","Endoplasmic Reticulum Stress and Disease","Lysosomal Storage Disorders Research","Chemistry","Medicine","Biology"],"mesh_terms":[],"keywords":["Secretion","Endoplasmic reticulum","Signal peptide","Secretory protein","Protein Sorting Signals","Secretory pathway","Cell biology","Protein folding","Transport protein","ER retention","Membrane protein","Biology","Protein targeting","Peptide sequence","Biochemistry","Membrane","Golgi apparatus","Gene","Protein translocation","Neurodegenerative diseases","Protein Quality Control","Chaperone-mediated Autophagy","Unconventional Protein Secretion","Misfolding-associated Protein Secretion (Maps)","Endo-lysosome","Intercellular Transmission Of Proteins"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-07T21:08:48.634162Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}