{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T06:57:40Z","timestamp":1787986660621,"version":"build-2784847793"},"reference-count":180,"publisher":"Portland Press Ltd.","issue":"5","license":[{"start":{"date-parts":[[2022,4,8]],"date-time":"2022-04-08T00:00:00Z","timestamp":1649376000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2022,5,27]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Lysosomes are key regulators of many fundamental cellular processes such as metabolism, autophagy, immune response, cell signalling and plasma membrane repair. These highly dynamic organelles are composed of various membrane and soluble proteins, which are essential for their proper functioning. The soluble proteins include numerous proteases, glycosidases and other hydrolases, along with activators, required for catabolism. The correct sorting of soluble lysosomal proteins is crucial to ensure the proper functioning of lysosomes and is achieved through the coordinated effort of many sorting receptors, resident ER and Golgi proteins, and several cytosolic components. Mutations in a number of proteins involved in sorting soluble proteins to lysosomes result in human disease. These can range from rare diseases such as lysosome storage disorders, to more prevalent ones, such as Alzheimer\u2019s disease, Parkinson\u2019s disease and others, including rare neurodegenerative diseases that affect children. In this review, we discuss the mechanisms that regulate the sorting of soluble proteins to lysosomes and highlight the effects of mutations in this pathway that cause human disease. More precisely, we will review the route taken by soluble lysosomal proteins from their translation into the ER, their maturation along the Golgi apparatus, and sorting at the trans-Golgi network. We will also highlight the effects of mutations in this pathway that cause human disease.<\/jats:p>","DOI":"10.1042\/bsr20211856","type":"journal-article","created":{"date-parts":[[2022,4,8]],"date-time":"2022-04-08T09:28:27Z","timestamp":1649410107000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Mechanisms regulating the sorting of soluble lysosomal proteins"],"prefix":"10.1042","volume":"42","author":[{"given":"\u0130\u00e7ten","family":"Mera\u015f","sequence":"first","affiliation":[{"name":"Centre Armand-Frappier Sant\u00e9 Biotechnologie, Institut national de la recherche scientifique, Laval, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juliette","family":"Maes","sequence":"additional","affiliation":[{"name":"Centre Armand-Frappier Sant\u00e9 Biotechnologie, Institut national de la recherche scientifique, Laval, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3312-9594","authenticated-orcid":false,"given":"Stephane","family":"Lefrancois","sequence":"additional","affiliation":[{"name":"Centre Armand-Frappier Sant\u00e9 Biotechnologie, Institut national de la recherche scientifique, Laval, Canada"},{"name":"Department of Anatomy and Cell Biology, McGill University, Montreal, Canada H3A 0C7"},{"name":"Centre d\u2019Excellence en Recherche sur les Maladies Orphelines - Fondation Courtois (CERMO-FC), Universit\u00e9 du Qu\u00e9bec \u00e0 Montr\u00e9al (UQAM), Montr\u00e9al, Canada H2X 3Y7"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2022,5,13]]},"reference":[{"key":"2022051307530945000_B1","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1146\/annurev-neuro-080317-061804","article-title":"Lysosomes and brain health","volume":"41","author":"Sharma","year":"2018","journal-title":"Annu. 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