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10.1242/jcs.198267 http://scihub22266oqcxt.onion/10.1242/jcs.198267 C5450233!5450233 !28302907     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28302907 &cmd=llinks): Failed to open stream: HTTP request failed! 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SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain |pdf=|usr=}}{{28302907 }} gab.com Text SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=28302907 #FOAvip The molecular interplay between cargo recognition and regulation of the activity of the kinesin-1 microtubule motor is not well understood. Using the lysosome adaptor SKIP (also known as PLEKHM2) as model cargo, we show that the kinesin heavy chains (KHCs), in addition to the kinesin light chains (KLCs), can recognize tryptophan-acidic-binding determinants on the cargo when presented in the context of an extended KHC-interacting domain. Mutational separation of KHC and KLC binding shows that both interactions are important for SKIP-kinesin-1 interaction in vitro and that KHC binding is important for lysosome transport in vivo However, in the absence of KLCs, SKIP can only bind to KHC when autoinhibition is relieved, suggesting that the KLCs gate access to the KHCs. We propose a model whereby tryptophan-acidic cargo is first recognized by KLCs, resulting in destabilization of KHC autoinhibition. This primary event then makes accessible a second SKIP-binding site on the KHC C-terminal tail that is adjacent to the autoinhibitory IAK region. Thus, cargo recognition and concurrent activation of kinesin-1 proceed in hierarchical stepwise fashion driven by a dynamic network of inter- and intra-molecular interactions. Twit Text FOAVip SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=28302907 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28302907 #FOAvip English Wikipedia <ref>{{Cite pmid|28302907 }}</ref> SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain #MMPMID28302907 Sanger A ; Yip YY ; Randall TS ; Pernigo S ; Steiner RA ; Dodding MP J Cell Sci 2017[May]; 130 (9 ): 1637-1651 PMID28302907 show ga The molecular interplay between cargo recognition and regulation of the activity of the kinesin-1 microtubule motor is not well understood. Using the lysosome adaptor SKIP (also known as PLEKHM2) as model cargo, we show that the kinesin heavy chains (KHCs), in addition to the kinesin light chains (KLCs), can recognize tryptophan-acidic-binding determinants on the cargo when presented in the context of an extended KHC-interacting domain. Mutational separation of KHC and KLC binding shows that both interactions are important for SKIP-kinesin-1 interaction in vitro and that KHC binding is important for lysosome transport in vivo However, in the absence of KLCs, SKIP can only bind to KHC when autoinhibition is relieved, suggesting that the KLCs gate access to the KHCs. We propose a model whereby tryptophan-acidic cargo is first recognized by KLCs, resulting in destabilization of KHC autoinhibition. This primary event then makes accessible a second SKIP-binding site on the KHC C-terminal tail that is adjacent to the autoinhibitory IAK region. Thus, cargo recognition and concurrent activation of kinesin-1 proceed in hierarchical stepwise fashion driven by a dynamic network of inter- and intra-molecular interactions. |Adaptor Proteins, Signal Transducing/chemistry/*metabolism [MESH] |Amino Acid Motifs [MESH] |Amino Acid Sequence [MESH] |Animals [MESH] |Binding Sites [MESH] |Calcium-Binding Proteins/metabolism [MESH] |HeLa Cells [MESH] |Humans [MESH] |Kinesins/*metabolism [MESH] |Lysosomes/*metabolism [MESH] |Mutation/genetics [MESH] |Protein Binding [MESH] |Protein Domains [MESH]SKIP controls lysosome positioning using a composite kinesin-1 heavy a(epmc).pdf DeepDyve Pubget Overpricing