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| Subject Categories: Membranes & Transport | Structural Biology |
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| The EMBO Journal
(2007) 26, 3709–3719, doi:10.1038/sj.emboj.7601800 Published online 19 July 2007 |
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| The structural basis of novel endosome anchoring activity of KIF16B kinesin |
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| Nichole R Blatner1, Michael I Wilson2, Cai Lei3, Wanjin Hong3, Diana Murray4, Roger L Williams2 and Wonhwa Cho1 |
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1 Department of Chemistry, University of Illinois at Chicago, Chicago, IL, USA 2 MRC Laboratory of Molecular Biology, Cambridge, UK 3 Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore, Singapore 4 Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY, USA To whom correspondence should be addressed Wonhwa Cho, Department of Chemistry (M/C 111), University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL 60607, USA. Tel.: +1 312 996 4883; Fax: +1 312 996 0431; E-mail: wcho@uic.edu Received 22 March 2007; Accepted 26 June 2007; Published online 19 July 2007. |
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| Abstract |
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| KIF16B is a newly identified kinesin that regulates the intracellular motility of early endosomes. KIF16B is unique among kinesins in that its cargo binding is mediated primarily by the strong interaction of its PX domain with endosomal lipids. To elucidate the structural basis of this unique endosomal anchoring activity of KIF16B-PX, we determined the crystal structure of the PX domain and performed in vitro and cellular membrane binding measurements for KIF16B-PX and mutants. The most salient structural feature of KIF16B-PX is that two neighboring residues, L1248 and F1249, on the membrane-binding surface form a protruding hydrophobic stalk with a large solvent-accessible surface area. This unique structure, arising from the complementary stacking of the two side chains and the local conformation, allows strong hydrophobic membrane interactions and endosome tethering. The presence of similar hydrophobic pairs in the amino-acid sequences of other membrane-binding domains and proteins suggests that the same structural motif may be shared by other membrane-binding proteins, whose physiological functions depend on strong hydrophobic membrane interactions. |
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| Keywords: crystal structure, endosome anchoring, kinesin, PX domain |
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Top of page MORE ARTICLES LIKE THISThese links to content published by NPG are automatically generated NEWS AND VIEWSPX domains: attracted by phosphoinositides Nature Cell Biology News and Views (01 Aug 2001) New candidates for vesicle coat proteins Nature Cell Biology News and Views (01 May 2004) RESEARCHThe structural basis of novel endosome anchoring activity of KIF16B kinesin The EMBO Journal Article The EMBO Journal Article (01 Oct 2002) |
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