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http://hdl.handle.net/10201/36010
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Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Canuel, Maryssa | es |
dc.contributor.author | Libin, Yuan | es |
dc.contributor.author | Morales, Carlos R. | - |
dc.date.accessioned | 2013-09-24T11:34:31Z | - |
dc.date.available | 2013-09-24T11:34:31Z | - |
dc.date.issued | 2009 | - |
dc.identifier.issn | 0213-3911 | es |
dc.identifier.uri | http://hdl.handle.net/10201/36010 | - |
dc.description.abstract | The 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.format | application/pdf | es |
dc.format.extent | 12 | es |
dc.language | eng | es |
dc.publisher | Murcia : F. Hernández | es |
dc.relation.ispartof | Histology and histopathology | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.subject | Sorting receptors | es |
dc.subject | Lysosomes | es |
dc.subject.other | 576 - Biología celular y subcelular. Citología | es |
dc.title | The interactomics of sortilin: an ancient lysosomal receptor evolving new functions | es |
dc.type | info:eu-repo/semantics/article | es |
Aparece en las colecciones: | Vol.24, nº4 (2009) |
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Fichero | Descripción | Tamaño | Formato | |
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The interactomics of sortilin an ancient lysosomal receptor evolving new functions.pdf | 1,92 MB | Adobe PDF | ![]() Visualizar/Abrir |
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