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http://purl.uniprot.org/citations/22284051http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22284051http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22284051http://www.w3.org/2000/01/rdf-schema#comment"Rabankyrin-5 (Rank-5) has been implicated as an effector of the small GTPase Rab5 and plays an important role in macropinocytosis. We have now identified Rank-5 as an interaction partner for the recycling regulatory protein, Eps15 homology domain 1 (EHD1). We have demonstrated this interaction by glutathione S-transferase-pulldown, yeast two-hybrid assay, isothermal calorimetry and co-immunoprecipitation, and found that the binding occurs between the EH domain of EHD1 and the NPFED motif of Rank-5. Similar to EHD1, we found that Rank-5 colocalizes and interacts with components of the retromer complex such as vacuolar protein sorting 26 (Vps26), suggesting a role for Rank-5 in retromer-based transport. Indeed, depletion of Rank-5 causes mislocalization of Vps26 and affects both the retrieval of mannose 6-phosphate receptor transport to the Golgi from endosomes and biosynthetic transport. Moreover, Rank-5 is required for normal retromer distribution, as overexpression of a wild-type Rank-5-small interfering RNA-resistant construct rescues retromer mislocalization. Finally, we show that depletion of either Rank-5 or EHD1 impairs secretion of vesicular stomatitis virus glycoprotein. Overall, our data identify a new interaction between Rank-5 and EHD1, and novel endocytic regulatory roles that include retromer-based transport and secretion."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.org/dc/terms/identifier"doi:10.1111/j.1600-0854.2012.01334.x"xsd:string
http://purl.uniprot.org/citations/22284051http://purl.org/dc/terms/identifier"doi:10.1111/j.1600-0854.2012.01334.x"xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Zhang J."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Zhang J."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Caplan S."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Caplan S."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Marky L.A."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Marky L.A."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Naslavsky N."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Naslavsky N."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Prislan I."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Prislan I."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Reiling C."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Reiling C."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Reinecke J.B."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Reinecke J.B."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Sorgen P.L."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/author"Sorgen P.L."xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/name"Traffic"xsd:string
http://purl.uniprot.org/citations/22284051http://purl.uniprot.org/core/name"Traffic"xsd:string