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http://purl.uniprot.org/citations/15882442http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15882442http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15882442http://www.w3.org/2000/01/rdf-schema#comment"The spatial organization of organelles within a cell is dependent on microtubules. Recently, members of the Hook family of proteins have been proposed to function in linking organelles to microtubules. We report the identification of a completely novel protein family, the Hook-related protein (HkRP) family, from which the Hook proteins have diverged. Bioinformatic analysis of the HkRP family revealed several conserved domains, including a unique C-terminal HkRP domain. The central region of each protein is comprised of an extensive coiled-coil domain, and the N-terminus contains a putative microtubule-binding domain. This domain has been shown to bind microtubules in the Hook protein and show that the HkRP1 protein is microtubule-associated. While endogenous HkRP1 has no distinct organelle association, expression of the C-terminal membrane-binding domain suggests a function of the HkRP1 in early endosome. Ultrastructural studies reveal that expression of the C-terminal HkRP1 domain causes an accumulation of internal membranes with an electron-dense coat. Co-localization studies show a concomitant redistribution of the early endosome marker sorting-nexin 1 but not the early endosome antigen-1 (EEA1). The steady-state distribution of the epidermal growth factor receptor is also specifically disrupted by expression of the C-terminal domain. We propose that HkRP1 is involved in the process of tubulation of sorting nexin-1 positive membranes from early endosome subdomains."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.org/dc/terms/identifier"doi:10.1111/j.1600-0854.2005.00289.x"xsd:string
http://purl.uniprot.org/citations/15882442http://purl.org/dc/terms/identifier"doi:10.1111/j.1600-0854.2005.00289.x"xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"James D.E."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"James D.E."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Martin S."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Martin S."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Teasdale R.D."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Teasdale R.D."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Simpson F."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Simpson F."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Parton R.G."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Parton R.G."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Kerr M."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Kerr M."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Wicking C."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Wicking C."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Evans T.M."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/author"Evans T.M."xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/name"Traffic"xsd:string
http://purl.uniprot.org/citations/15882442http://purl.uniprot.org/core/name"Traffic"xsd:string