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10.1128/MCB.00020-16 http://scihub22266oqcxt.onion/10.1128/MCB.00020-16 C4959310!4959310 !27044863     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27044863 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Cell+Biol 2016 ; 36 (11 ): 1639-54 Nephropedia Template TP {{tp|p=27044863 |t=2016. Structural Analysis of the Myo1c and Neph1 Complex Provides Insight into the Intracellular Movement of Neph1 |pdf=|usr=}}{{27044863 }} gab.com Text Structural Analysis of the Myo1c and Neph1 Complex Provides Insight into the Intracellular Movement of Neph1 JO: Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27044863 #FOAvip The Myo1c motor functions as a cargo transporter supporting various cellular events, including vesicular trafficking, cell migration, and stereociliary movements of hair cells. Although its partial crystal structures were recently described, the structural details of its interaction with cargo proteins remain unknown. This study presents the first structural demonstration of a cargo protein, Neph1, attached to Myo1c, providing novel insights into the role of Myo1c in intracellular movements of this critical slit diaphragm protein. Using small angle X-ray scattering studies, models of predominant solution conformation of unliganded full-length Myo1c and Myo1c bound to Neph1 were constructed. The resulting structures show an extended S-shaped Myo1c with Neph1 attached to its C-terminal tail. Importantly, binding of Neph1 did not induce a significant shape change in Myo1c, indicating this as a spontaneous process or event. Analysis of interaction surfaces led to the identification of a critical residue in Neph1 involved in binding to Myo1c. Indeed, a point mutant from this site abolished interaction between Neph1 and Myo1c when tested in the in vitro and in live-cell binding assays. Live-cell imaging, including fluorescence recovery after photobleaching, provided further support for the role of Myo1c in intracellular vesicular movement of Neph1 and its turnover at the membrane. Twit Text FOAVip Structural Analysis of the Myo1c and Neph1 Complex Provides Insight into the Intracellular Movement of Neph1 ????Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27044863 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27044863 #FOAvip English Wikipedia <ref>{{Cite pmid|27044863 }}</ref> Structural Analysis of the Myo1c and Neph1 Complex Provides Insight into the Intracellular Movement of Neph1 #MMPMID27044863 Arif E ; Sharma P ; Solanki A ; Mallik L ; Rathore YS ; Twal WO ; Nath SK ; Gandhi D ; Holzman LB ; Ostap EM ; Ashish ; Nihalani D Mol Cell Biol 2016[Jun]; 36 (11 ): 1639-54 PMID27044863 show ga The Myo1c motor functions as a cargo transporter supporting various cellular events, including vesicular trafficking, cell migration, and stereociliary movements of hair cells. Although its partial crystal structures were recently described, the structural details of its interaction with cargo proteins remain unknown. This study presents the first structural demonstration of a cargo protein, Neph1, attached to Myo1c, providing novel insights into the role of Myo1c in intracellular movements of this critical slit diaphragm protein. Using small angle X-ray scattering studies, models of predominant solution conformation of unliganded full-length Myo1c and Myo1c bound to Neph1 were constructed. The resulting structures show an extended S-shaped Myo1c with Neph1 attached to its C-terminal tail. Importantly, binding of Neph1 did not induce a significant shape change in Myo1c, indicating this as a spontaneous process or event. Analysis of interaction surfaces led to the identification of a critical residue in Neph1 involved in binding to Myo1c. Indeed, a point mutant from this site abolished interaction between Neph1 and Myo1c when tested in the in vitro and in live-cell binding assays. Live-cell imaging, including fluorescence recovery after photobleaching, provided further support for the role of Myo1c in intracellular vesicular movement of Neph1 and its turnover at the membrane. |Binding Sites [MESH] |Cells, Cultured [MESH] |Humans [MESH] |Membrane Proteins/*chemistry/genetics/*metabolism [MESH] |Models, Molecular [MESH] |Myosin Type I/*chemistry/*metabolism [MESH] |Podocytes/metabolism/ultrastructure [MESH] |Point Mutation [MESH] |Protein Binding [MESH] |Protein Transport [MESH] |Scattering, Small Angle [MESH]Structural Analysis of the Myo1c and Neph1 Complex Provides Insight in(epmc).pdf DeepDyve Pubget Overpricing