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The interactomics of sortilin: an ancient lysosomal receptor evolving new functions

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dc.contributor.authorCanuel, Maryssaes
dc.contributor.authorLibin, Yuanes
dc.contributor.authorMorales, Carlos R.
dc.date.accessioned2013-09-24T11:34:31Z
dc.date.available2013-09-24T11:34:31Z
dc.date.issued2009
dc.description.abstractThe delivery of soluble lysosomal proteins to the lysosomes is dependent primarily on the mannose 6- phosphate receptor (MPR). The MPR has been demonstrated to attain the early endosomes via a process that requires the interaction of its cytosolic domain with the GGA and AP-1 adaptor proteins. Additionally, the MPR can be recycled back to the trans-Golgi network (TGN) through its interaction with the retromer complex. Interestingly, in I-cell disease (ICD), in which the MPR pathway is non-functional, many soluble lysosomal proteins continue to traffic to the lysosomes. This observation led to the discovery that sortilin is responsible for the MPR-independent targeting of the sphingolipid activator proteins (SAPs) and acid sphingomyelinase (ASM). More recently, our laboratory has tested the hypothesis that sortilin is also capable of sorting a variety of cathepsins that exhibit varying degrees of MPR-independent transport. We have demonstrated that the transport of cathepsin D is partially dependent upon sortilin, that cathepsin H requires sortilin, and that cathepsins K and L attain the lysosomes in a sortilin-independent fashion. As a type-1 receptor, sortilin also has numerous cytosolic binding partners. It has been observed that like the MPR, the anterograde trafficking of sortilin and its cargo require both GGAs and AP-1. Similarly, the retrograde recycling pathway of sortilin also involves an interaction with retromer through a YXXf site in the cytosolic tail of sortilin. In conclusion, the cytosolic domains of sortilin and MPR possess a high degree of functional homology and both receptors share a conserved trafficking mechanism.es
dc.formatapplication/pdfes
dc.format.extent12es
dc.identifier.issn0213-3911es
dc.identifier.urihttp://hdl.handle.net/10201/36010
dc.languageenges
dc.publisherMurcia : F. Hernándezes
dc.relation.ispartofHistology and histopathologyes
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.subjectSorting receptorses
dc.subjectLysosomeses
dc.subject.other576 - Biología celular y subcelular. Citologíaes
dc.titleThe interactomics of sortilin: an ancient lysosomal receptor evolving new functionses
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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Histology and histopathology Vol.24, nº4 (2009)