Pneumatically-driven Microfluidic Device for Evaluating Active Transport by Kinesin Motor Protein

2016 ◽  
Vol 136 (9) ◽  
pp. 384-389
Author(s):  
Kazuya Fujimoto ◽  
Hirofumi Shintaku ◽  
Hidetoshi Kotera ◽  
Ryuji Yokokawa
Gene ◽  
2020 ◽  
Vol 760 ◽  
pp. 144989
Author(s):  
Anzana Parvin ◽  
Shuang-Li Hao ◽  
Fu-Qing Tan ◽  
Wan-Xi Yang

2012 ◽  
Vol 199 (5) ◽  
pp. 715-715
Author(s):  
Ben Short

A kinesin motor protein works with condensin and topoisomerase IIα to organize mitotic chromatin.


2005 ◽  
Vol 33 (6) ◽  
pp. 1279-1281 ◽  
Author(s):  
V. Kanamarlapudi

The ARF (ADP-ribosylation factor) family of small GTPases regulate intracellular membrane trafficking by cycling between an inactive GDP- and an active GTP-bound form. Among the six known mammalian ARFs (ARF1–ARF6), ARF6 is the least conserved and plays critical roles in membrane trafficking and cytoskeletal dynamics near the cell surface. Since ARFs have undetectable levels of intrinsic GTP binding and hydrolysis, they are totally dependent on extrinsic GEFs (guanine nucleotide-exchange factors) for GTP binding and GAPs (GTPase-activating proteins) for GTP hydrolysis. We have recently isolated a novel KIF (kinesin) motor protein (KIF13B) that binds to centaurin-α1, an ARF6GAP that binds to the second messenger PIP3 [PtdIns(3,4,5)P3]. KIFs transport intracellular vesicles and recognize their cargo by binding to proteins (receptors) localized on the surface of the cargo vesicles. Identification of centaurin-α1 as a KIF13B interactor suggests that KIF13B may transport ARF6 and/or PIP3 using centaurin-α1 as its receptor. This paper reviews the studies carried out to assess the interaction and regulation of centaurin-α1 by KIF13B.


2006 ◽  
Vol 95 (3) ◽  
pp. 533-538 ◽  
Author(s):  
Shu Taira ◽  
Yong-Zhong Du ◽  
Yuichi Hiratsuka ◽  
Kaoru Konishi ◽  
Tai Kubo ◽  
...  

2019 ◽  
Author(s):  
Kalpana Mandal ◽  
Katarzyna Pogoda ◽  
Satabdi Nandi ◽  
Samuel Mathieu ◽  
Amal Kasri ◽  
...  

SummaryMolecular motors play important roles in force generation, migration and intracellular trafficking. Changes in specific motor activities are altered in numerous diseases. KIF20A, a motor protein of the kinesin-6 family, is overexpressed in bladder cancer, and KIF20A levels correlate negatively with the clinical outcome. We report here a new role for the KIF20A kinesin motor protein in intracellular mechanics. Using optical tweezers to probe intracellular mechanics and surface AFM to probe cortical mechanics, we first confirm that bladder cells soften with increasing cancer grade. We then show that inhibiting KIF20A makes the intracellular environment softer for both high and low grade bladder cancer cells. Upon inhibition of KIF20A cortical stiffness also decreases in lower grade cells, while it surprisingly increases in higher grade malignant cells. Changes in cortical stiffness correlate with the interaction of KIF20A with myosin IIA. Moreover, KIF20A negatively regulates bladder cancer cell motility irrespective of the underlying substrate stiffness. Our results reveal a central role for a microtubule motor in cell mechanics and migration in the context of bladder cancer.


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