scholarly journals Virtual Issue on Protein Crowding and Stability

2021 ◽  
Vol 125 (38) ◽  
pp. 10649-10651
Author(s):  
Michael Feig
Keyword(s):  
2012 ◽  
Vol 102 (3) ◽  
pp. 322a ◽  
Author(s):  
Jeanne C. Stachowiak ◽  
Eva M. Schmid ◽  
Christopher J. Ryan ◽  
Hyoung S. Ann ◽  
Darryl Y. Sasaki ◽  
...  

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S259
Author(s):  
Takamitsu Morikawa ◽  
Keiko Yoshizawa ◽  
hideaki Fujita ◽  
Katsumi Imada ◽  
Takeharu Nagai ◽  
...  
Keyword(s):  

2013 ◽  
Vol 104 (2) ◽  
pp. 618a
Author(s):  
Carl C. Hayden ◽  
Jerin T. Jose ◽  
Justin R. Houser ◽  
David J. Busch ◽  
Jeanne C. Stachowiak

2017 ◽  
Vol 112 (3) ◽  
pp. 92a
Author(s):  
Zhenyong Wu ◽  
Oscar D. Bello ◽  
Sathish Thiyagarajan ◽  
Sarah M. Auclair ◽  
Wensi Vennekate ◽  
...  

Author(s):  
Verena Henrichs ◽  
Lenka Grycova ◽  
Cyril Barinka ◽  
Zuzana Nahacka ◽  
Jiri Neuzil ◽  
...  

SummaryIntracellular trafficking of organelles, driven by kinesin-1 stepping along microtubules, underpins essential processes including neuronal activity. In absence of other proteins on the microtubule surface, kinesin-1 performs micron-long runs. Under protein crowding conditions, however, kinesin-1 motility is drastically impeded. It is thus unclear how kinesin-1 acts as an efficient transporter in crowded intracellular environments. Here, we demonstrate that TRAK1 (Milton), an adaptor protein essential for mitochondrial trafficking, activates kinesin-1 and increases its robustness of stepping in protein crowding conditions. Interaction with TRAK1 i) facilitated kinesin-1 navigation around obstacles, ii) increased the probability of kinesin-1 passing through cohesive envelopes of tau and iii) increased the run length of kinesin-1 in cell lysate. We explain the enhanced motility by the observed direct interaction of TRAK1 with microtubules, providing an additional anchor for the kinesin-1-TRAK1 complex. We propose adaptor-mediated tethering as a mechanism regulating kinesin-1 motility in various cellular environments.


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