ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2010
A stretch of 17 amino acids in the prosaposin C terminus is critical for its binding to sortilin and targeting to lysosomes.
Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Prosaposin in CNS health and disease, metabolic stress and exercise adaptation.Journal of molecular medicine (Berlin, Germany) · 2026Review
- Prosaposin orchestrates a TGFβ1-driven paracrine loop between Schwann cells and gastric cancer to accelerate perineural invasion.Journal of experimental & clinical cancer research : CR · 2026Article
- Hyperglycosylation of prosaposin in tumor dendritic cells drives immune escape.Science (New York, N.Y.) · 2024Article
- Prosaposin in the rat oviductal epithelial cells.Cell and tissue research · 2021Article
- The role of disulfide bonds in a Solanum tuberosum saposin-like protein investigated using molecular dynamics.PloS one · 2020Article
- Lysosomal storage diseases.Translational science of rare diseases · 2017Review
- Prosaposin is a regulator of progranulin levels and oligomerization.Nature communications · 2016Article
- The protective role of prosaposin and its receptors in the nervous system.Brain research · 2014Review
- Structural and functional analysis of APOA5 mutations identified in patients with severe hypertriglyceridemia.Journal of lipid research · 2013Article
- The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting.Molecular and cellular biology · 2012Article
- Mechanisms and genetic determinants regulating sterol absorption, circulating LDL levels, and sterol elimination: implications for classification and disease risk.Journal of lipid research · 2011Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Prosaposin, the precursor of four lysosomal cofactors required for the hydrolysis of sphingolipids, is transported to the lysosomes via the alternative receptor, sortilin. In this study, we identified a specific domain of 17 amino acids within the C terminus of prosaposin involved in binding to this sorting receptor. We generated six prosaposin deletion constructs and examined the effect of truncation by coimmunoprecipitation and confocal microscopy. The experiments revealed that the first half of the prosaposin C terminus (aa 524-540), containing a saposin-like motif, was required and necessary to bind sortilin and to transport it to the lysosomes. Based on this result, we introduced twelve site-directed point mutations within the first half of the C terminus. Although the interaction of prosaposin with sortilin was pH dependent, the mutation of hydrophilic amino acids that usually modulate pH-dependent protein interactions did not affect the binding of prosaposin to sortilin. Conversely, a tryptophan (W530) and two cysteines (C528 and C536) were essential for its interaction with sortilin and for its transport to the lysosomes. In conclusion, our investigation demonstrates that a saposin-like motif within the first half of the prosaposin C terminus contains the sortilin recognition site.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.