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10.1083/jcb.201606092 http://scihub22266oqcxt.onion/10.1083/jcb.201606092 C5166503!5166503 !27920216     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27920216 &cmd=llinks): Failed to open stream: HTTP request failed! 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MOZART1 and ?-tubulin complex receptors are both required to turn ?-TuSC into an active microtubule nucleation template |pdf=|usr=}}{{27920216 }} gab.com Text MOZART1 and -tubulin complex receptors are both required to turn -TuSC into an active microtubule nucleation template JO: J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27920216 #FOAvip MOZART1/Mzt1 is required for the localization of ?-tubulin complexes to microtubule (MT)-organizing centers from yeast to human cells. Nevertheless, the molecular function of MOZART1/Mzt1 is largely unknown. Taking advantage of the minimal MT nucleation system of Candida albicans, we reconstituted the interactions of Mzt1, ?-tubulin small complex (?-TuSC), and ?-tubulin complex receptors (?-TuCRs) Spc72 and Spc110 in vitro. With affinity measurements, domain deletion, and swapping, we show that Spc110 and Mzt1 bind to distinct regions of the ?-TuSC. In contrast, both Mzt1 and ?-TuSC interact with the conserved CM1 motif of Spc110/Spc72. Spc110/Spc72 and Mzt1 constitute "oligomerization chaperones," cooperatively promoting and directing ?-TuSC oligomerization into MT nucleation-competent rings. Consistent with the functions of Mzt1, human MOZART1 directly interacts with the CM1-containing region of the ?-TuCR CEP215. MOZART1 depletion in human cells destabilizes the large ?-tubulin ring complex and abolishes CEP215(CM1)-induced ectopic MT nucleation. Together, we reveal conserved functions of MOZART1/Mzt1 through interactions with ?-tubulin complex subunits and ?-TuCRs. Twit Text FOAVip MOZART1 and -tubulin complex receptors are both required to turn -TuSC into an active microtubule nucleation template ????J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27920216 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27920216 #FOAvip English Wikipedia <ref>{{Cite pmid|27920216 }}</ref> MOZART1 and ?-tubulin complex receptors are both required to turn ?-TuSC into an active microtubule nucleation template #MMPMID27920216 Lin TC ; Neuner A ; Flemming D ; Liu P ; Chinen T ; Jäkle U ; Arkowitz R ; Schiebel E J Cell Biol 2016[Dec]; 215 (6 ): 823-840 PMID27920216 show ga MOZART1/Mzt1 is required for the localization of ?-tubulin complexes to microtubule (MT)-organizing centers from yeast to human cells. Nevertheless, the molecular function of MOZART1/Mzt1 is largely unknown. Taking advantage of the minimal MT nucleation system of Candida albicans, we reconstituted the interactions of Mzt1, ?-tubulin small complex (?-TuSC), and ?-tubulin complex receptors (?-TuCRs) Spc72 and Spc110 in vitro. With affinity measurements, domain deletion, and swapping, we show that Spc110 and Mzt1 bind to distinct regions of the ?-TuSC. In contrast, both Mzt1 and ?-TuSC interact with the conserved CM1 motif of Spc110/Spc72. Spc110/Spc72 and Mzt1 constitute "oligomerization chaperones," cooperatively promoting and directing ?-TuSC oligomerization into MT nucleation-competent rings. Consistent with the functions of Mzt1, human MOZART1 directly interacts with the CM1-containing region of the ?-TuCR CEP215. MOZART1 depletion in human cells destabilizes the large ?-tubulin ring complex and abolishes CEP215(CM1)-induced ectopic MT nucleation. Together, we reveal conserved functions of MOZART1/Mzt1 through interactions with ?-tubulin complex subunits and ?-TuCRs. |Candida albicans/*metabolism [MESH] |Fungal Proteins/chemistry/*metabolism [MESH] |Humans [MESH] |Microtubule-Associated Proteins/metabolism [MESH] |Microtubules/*metabolism [MESH] |Models, Biological [MESH] |Protein Binding [MESH] |Protein Domains [MESH] |Protein Multimerization [MESH] |Protein Stability [MESH] |Saccharomyces cerevisiae/metabolism [MESH] |Spindle Apparatus/metabolism [MESH] |Spindle Pole Bodies/metabolism [MESH]MOZART1 and ?-tubulin complex receptors are both required to turn ?-Tu(epmc).pdf DeepDyve Pubget Overpricing