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10.1091/mbc.E14-10-1477 http://scihub22266oqcxt.onion/10.1091/mbc.E14-10-1477 C4310740!4310740 !25473116     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 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\25473116 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Biol+Cell 2015 ; 26 (3 ): 495-505 Nephropedia Template TP {{tp|p=25473116 |t=2015. A novel role for WAVE1 in controlling actin network growth rate and architecture |pdf=|usr=}}{{25473116 }} gab.com Text A novel role for WAVE1 in controlling actin network growth rate and architecture JO: Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25473116 #FOAvip Branched actin filament networks in cells are assembled through the combined activities of Arp2/3 complex and different WASP/WAVE proteins. Here we used TIRF and electron microscopy to directly compare for the first time the assembly kinetics and architectures of actin filament networks produced by Arp2/3 complex and dimerized VCA regions of WAVE1, WAVE2, or N-WASP. WAVE1 produced strikingly different networks from WAVE2 or N-WASP, which comprised unexpectedly short filaments. Further analysis showed that the WAVE1-specific activity stemmed from an inhibitory effect on filament elongation both in the presence and absence of Arp2/3 complex, which was observed even at low stoichiometries of WAVE1 to actin monomers, precluding an effect from monomer sequestration. Using a series of VCA chimeras, we mapped the elongation inhibitory effects of WAVE1 to its WH2 ("V") domain. Further, mutating a single conserved lysine residue potently disrupted WAVE1's inhibitory effects. Taken together, our results show that WAVE1 has unique activities independent of Arp2/3 complex that can govern both the growth rates and architectures of actin filament networks. Such activities may underlie previously observed differences between the cellular functions of WAVE1 and WAVE2. Twit Text FOAVip A novel role for WAVE1 in controlling actin network growth rate and architecture ????Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25473116 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25473116 #FOAvip English Wikipedia <ref>{{Cite pmid|25473116 }}</ref> A novel role for WAVE1 in controlling actin network growth rate and architecture #MMPMID25473116 Sweeney MO ; Collins A ; Padrick SB ; Goode BL Mol Biol Cell 2015[Feb]; 26 (3 ): 495-505 PMID25473116 show ga Branched actin filament networks in cells are assembled through the combined activities of Arp2/3 complex and different WASP/WAVE proteins. Here we used TIRF and electron microscopy to directly compare for the first time the assembly kinetics and architectures of actin filament networks produced by Arp2/3 complex and dimerized VCA regions of WAVE1, WAVE2, or N-WASP. WAVE1 produced strikingly different networks from WAVE2 or N-WASP, which comprised unexpectedly short filaments. Further analysis showed that the WAVE1-specific activity stemmed from an inhibitory effect on filament elongation both in the presence and absence of Arp2/3 complex, which was observed even at low stoichiometries of WAVE1 to actin monomers, precluding an effect from monomer sequestration. Using a series of VCA chimeras, we mapped the elongation inhibitory effects of WAVE1 to its WH2 ("V") domain. Further, mutating a single conserved lysine residue potently disrupted WAVE1's inhibitory effects. Taken together, our results show that WAVE1 has unique activities independent of Arp2/3 complex that can govern both the growth rates and architectures of actin filament networks. Such activities may underlie previously observed differences between the cellular functions of WAVE1 and WAVE2. |Actin Cytoskeleton/chemistry/metabolism/*ultrastructure [MESH] |Actin-Related Protein 2-3 Complex/metabolism [MESH] |Animals [MESH] |Cattle [MESH] |Humans [MESH] |Microscopy, Electron [MESH] |Microscopy, Fluorescence [MESH] |Polymerization [MESH] |Protein Structure, Tertiary [MESH]A novel role for WAVE1 in controlling actin network growth rate and ar(epmc).pdf DeepDyve Pubget Overpricing