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10.1016/j.devcel.2018.05.032 http://scihub22266oqcxt.onion/10.1016/j.devcel.2018.05.032 C6035287!6035287!29937387     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       Dev+Cell 2018 ; 46 (1): 40-58.e8 Nephropedia Template TP {{tp|p=29937387|t=2018. CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain |pdf=|usr=}}{{29937387}} gab.com Text CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain JO: Dev Cell http://www.kidney.de/pget.php?&tw=1&pmid=29937387 #FOAvip The dynamic instability of microtubules plays a key role in controlling their organization and function, but the cellular mechanisms regulating this process are poorly understood. Here, we show that cytoplasmic linker-associated proteins (CLASPs) suppress transitions from microtubule growth to shortening, termed catastrophes, including those induced by microtubule-destabilizing agents and physical barriers. Mammalian CLASPs encompass three TOG-like domains, TOG1, TOG2, and TOG3, none of which bind to free tubulin. TOG2 is essential for catastrophe suppression, whereas TOG3 mildly enhances rescues but cannot suppress catastrophes. These functions are inhibited by the C-terminal domain of CLASP2, while the TOG1 domain can release this auto-inhibition. TOG2 fused to a positively charged microtubule-binding peptide autonomously accumulates at growing but not shrinking ends, suppresses catastrophes, and stimulates rescues. CLASPs suppress catastrophes by stabilizing growing microtubule ends, including incomplete ones, preventing their depolymerization and promoting their recovery into complete tubes. TOG2 domain is the key determinant of these activities. Twit Text FOAVip CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain ????Dev Cell http://www.kidney.de/pget.php?&tw=1&pmid=29937387 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29937387 #FOAvip English Wikipedia <ref>{{Cite pmid|29937387}}</ref> CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain #MMPMID29937387 Aher A; Kok M; Sharma A; Rai A; Olieric N; Rodriguez-Garcia R; Katrukha EA; Weinert T; Olieric V; Kapitein LC; Steinmetz MO; Dogterom M; Akhmanova A Dev Cell 2018[Jul]; 46 (1): 40-58.e8 PMID29937387show ga The dynamic instability of microtubules plays a key role in controlling their organization and function, but the cellular mechanisms regulating this process are poorly understood. Here, we show that cytoplasmic linker-associated proteins (CLASPs) suppress transitions from microtubule growth to shortening, termed catastrophes, including those induced by microtubule-destabilizing agents and physical barriers. Mammalian CLASPs encompass three TOG-like domains, TOG1, TOG2, and TOG3, none of which bind to free tubulin. TOG2 is essential for catastrophe suppression, whereas TOG3 mildly enhances rescues but cannot suppress catastrophes. These functions are inhibited by the C-terminal domain of CLASP2, while the TOG1 domain can release this auto-inhibition. TOG2 fused to a positively charged microtubule-binding peptide autonomously accumulates at growing but not shrinking ends, suppresses catastrophes, and stimulates rescues. CLASPs suppress catastrophes by stabilizing growing microtubule ends, including incomplete ones, preventing their depolymerization and promoting their recovery into complete tubes. TOG2 domain is the key determinant of these activities. äCLASP Suppresses Microtubule Catastrophes through a Single TOG Domain (epmc).pdf DeepDyve Pubget Overpricing