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10.1091/mbc.E16-11-0764 http://scihub22266oqcxt.onion/10.1091/mbc.E16-11-0764 C5231900!5231900 !27852901     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27852901 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Mol+Biol+Cell 2017 ; 28 (2 ): 322-332 Nephropedia Template TP {{tp|p=27852901 |t=2017. Multivalent Rab interactions determine tether-mediated membrane fusion |pdf=|usr=}}{{27852901 }} gab.com Text Multivalent Rab interactions determine tether-mediated membrane fusion JO: Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=27852901 #FOAvip Membrane fusion at endomembranes requires cross-talk between Rab GTPases and tethers to drive SNARE-mediated lipid bilayer mixing. Several tethers have multiple Rab-binding sites with largely untested function. Here we dissected the lysosomal HOPS complex as a tethering complex with just two binding sites for the Rab7-like Ypt7 protein to determine their relevance for fusion. Using tethering and fusion assays combined with HOPS mutants, we show that HOPS-dependent fusion requires both Rab-binding sites, with Vps39 being the stronger Ypt7 interactor than Vps41. The intrinsic amphipathic lipid packaging sensor (ALPS) motif within HOPS Vps41, a target of the vacuolar kinase Yck3, is dispensable for tethering and fusion but can affect tethering if phosphorylated. In combination, our data demonstrate that a multivalent tethering complex uses its two Rab bindings to determine the place of SNARE assembly and thus fusion at endomembranes. Twit Text FOAVip Multivalent Rab interactions determine tether-mediated membrane fusion ????Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=27852901 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27852901 #FOAvip English Wikipedia <ref>{{Cite pmid|27852901 }}</ref> Multivalent Rab interactions determine tether-mediated membrane fusion #MMPMID27852901 Lürick A ; Gao J ; Kuhlee A ; Yavavli E ; Langemeyer L ; Perz A ; Raunser S ; Ungermann C Mol Biol Cell 2017[Jan]; 28 (2 ): 322-332 PMID27852901 show ga Membrane fusion at endomembranes requires cross-talk between Rab GTPases and tethers to drive SNARE-mediated lipid bilayer mixing. Several tethers have multiple Rab-binding sites with largely untested function. Here we dissected the lysosomal HOPS complex as a tethering complex with just two binding sites for the Rab7-like Ypt7 protein to determine their relevance for fusion. Using tethering and fusion assays combined with HOPS mutants, we show that HOPS-dependent fusion requires both Rab-binding sites, with Vps39 being the stronger Ypt7 interactor than Vps41. The intrinsic amphipathic lipid packaging sensor (ALPS) motif within HOPS Vps41, a target of the vacuolar kinase Yck3, is dispensable for tethering and fusion but can affect tethering if phosphorylated. In combination, our data demonstrate that a multivalent tethering complex uses its two Rab bindings to determine the place of SNARE assembly and thus fusion at endomembranes. |Binding Sites [MESH] |Endosomes/metabolism [MESH] |Membrane Fusion/*physiology [MESH] |Phosphorylation [MESH] |Protein Binding [MESH] |Protein Transport/physiology [MESH] |SNARE Proteins/metabolism [MESH] |Saccharomyces cerevisiae Proteins/*metabolism/physiology [MESH] |Saccharomyces cerevisiae/metabolism [MESH] |Vacuoles/metabolism [MESH] |Vesicular Transport Proteins/metabolism [MESH]Multivalent Rab interactions determine tether-mediated membrane fusion(epmc).pdf DeepDyve Pubget Overpricing