scholarly journals Cryo-EM structure of a microtubule-bound parasite kinesin motor and implications for its mechanism and inhibition

2021 ◽  
pp. 101063
Author(s):  
Alexander D. Cook ◽  
Anthony J. Roberts ◽  
Joseph Atherton ◽  
Rita Tewari ◽  
Maya Topf ◽  
...  
Keyword(s):  
Kinesin Motor

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
Keyword(s):  
Active Transport ◽  
Microfluidic Device ◽  
Motor Protein ◽  
Kinesin Motor

Inhibition of kinesin motor protein KIFC1 by AZ82 induces multipolar mitosis and apoptosis in prostate cancer cell

Gene ◽  
2020 ◽  
Vol 760 ◽  
pp. 144989
Author(s):  
Anzana Parvin ◽  
Shuang-Li Hao ◽  
Fu-Qing Tan ◽  
Wan-Xi Yang
Keyword(s):  
Prostate Cancer ◽  
Cancer Cell ◽  
Prostate Cancer Cell ◽  
Motor Protein ◽  
Kinesin Motor ◽  
Multipolar Mitosis

scholarly journals Remote control of microtubule plus-end dynamics and function from the minus-end

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Xiuzhen Chen ◽  
Lukas A Widmer ◽  
Marcel M Stangier ◽  
Michel O Steinmetz ◽  
Jörg Stelling ◽  
...  
Keyword(s):  
Remote Control ◽  
Mother Cell ◽  
Spindle Pole ◽  
Kinesin Motor ◽  
Random Lattice ◽  
Spindle Pole Bodies ◽  
Dividing Cells ◽  
Dynamics And Function ◽  
And Function ◽  
Microtubule Function

In eukaryotes, the organization and function of the microtubule cytoskeleton depend on the allocation of different roles to individual microtubules. For example, many asymmetrically dividing cells differentially specify microtubule behavior at old and new centrosomes. Here we show that yeast spindle pole bodies (SPBs, yeast centrosomes) differentially control the plus-end dynamics and cargoes of their astral microtubules, remotely from the minus-end. The old SPB recruits the kinesin motor protein Kip2, which then translocates to the plus-end of the emanating microtubules, promotes their extension and delivers dynein into the bud. Kip2 recruitment at the SPB depends on Bub2 and Bfa1, and phosphorylation of cytoplasmic Kip2 prevents random lattice binding. Releasing Kip2 of its control by SPBs equalizes its distribution, the length of microtubules and dynein distribution between the mother cell and its bud. These observations reveal that microtubule organizing centers use minus to plus-end directed remote control to individualize microtubule function.

scholarly journals The mechanism of kinesin inhibition by kinesin-binding protein

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Joseph Atherton ◽  
Jessica JA Hummel ◽  
Natacha Olieric ◽  
Julia Locke ◽  
Alejandro Peña ◽  
...  
Keyword(s):  
Cell Function ◽  
Binding Protein ◽  
Eukaryotic Cell ◽  
Motor Domain ◽  
Tetratricopeptide Repeat ◽  
Kinesin Motor ◽  
Temporal Regulation ◽  
Cryo Electron Microscopy ◽  
Local Environments ◽  
Binding Surface

Subcellular compartmentalisation is necessary for eukaryotic cell function. Spatial and temporal regulation of kinesin activity is essential for building these local environments via control of intracellular cargo distribution. Kinesin-binding protein (KBP) interacts with a subset of kinesins via their motor domains, inhibits their microtubule (MT) attachment, and blocks their cellular function. However, its mechanisms of inhibition and selectivity have been unclear. Here we use cryo-electron microscopy to reveal the structure of KBP and of a KBP–kinesin motor domain complex. KBP is a tetratricopeptide repeat-containing, right-handed α-solenoid that sequesters the kinesin motor domain’s tubulin-binding surface, structurally distorting the motor domain and sterically blocking its MT attachment. KBP uses its α-solenoid concave face and edge loops to bind the kinesin motor domain, and selected structure-guided mutations disrupt KBP inhibition of kinesin transport in cells. The KBP-interacting motor domain surface contains motifs exclusively conserved in KBP-interacting kinesins, suggesting a basis for kinesin selectivity.

scholarly journals A non-canonical function for Centromere-associated protein-E (CENP-E) controls centrosome integrity and orientation of cell division

2020 ◽  
Author(s):  
Mikito Owa ◽  
Brian Dynlacht
Keyword(s):  
Cell Division ◽  
Mitotic Arrest ◽  
Canonical Function ◽  
Kinesin Motor ◽  
Cell Divisions ◽  
Pericentriolar Material ◽  
Conventional Methods ◽  
In Cells

SummaryCentromere-associated protein-E (CENP-E) is a kinesin motor localizing at kinetochores. Although its mitotic functions have been well studied, it has been challenging to investigate direct consequences of CENP-E removal using conventional methods because CENP-E depletion results in mitotic arrest. In this study, we harnessed an auxin-inducible degron system to achieve acute degradation of CENP-E. We revealed a kinetochore-independent role for CENP-E that removes pericentriolar material 1 (PCM1) from centrosomes in G2 phase. After acute loss of CENP-E, centrosomal Polo-like kinase 1 (Plk1) is sequestered by accumulated PCM1, resulting in aberrant phosphorylation and destabilization of centrosomes, which triggers loss of astral microtubules and oblique cell divisions. Furthermore, we also observed centrosome and cell division defects in cells from a microcephaly patient with mutations in CENPE. Orientation of cell division is deregulated in some microcephalic patients, and our unanticipated findings provide a unifying principle that explains how microcephaly can result from centrosomal defects.

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