Intrinsically disordered domain of kinesin-3 Kif14 enables unique functional diversity

2020 ◽  
Author(s):  
Benjamin Craske
Keyword(s):  
Functional Diversity ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Domain

scholarly journals Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity

2020 ◽  
Vol 30 (17) ◽  
pp. 3342-3351.e5 ◽  
Author(s):  
Ilia Zhernov ◽  
Stefan Diez ◽  
Marcus Braun ◽  
Zdenek Lansky
Keyword(s):  
Functional Diversity ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Domain

scholarly journals One domain fits all: Using disordered regions to sequester misfolded proteins

2018 ◽  
Vol 217 (4) ◽  
pp. 1173-1175 ◽  
Author(s):  
Edgar E. Boczek ◽  
Simon Alberti
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Adenosine Triphosphate ◽  
Small Heat Shock Proteins ◽  
Misfolded Proteins ◽  
Protein Deposition ◽  
Intrinsically Disordered ◽  
Cell Biol ◽  
Shock Proteins ◽  
Intrinsically Disordered Domain

Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to bind and sequester misfolded proteins in protein deposition sites.

scholarly journals NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B

2017 ◽  
Vol 292 (44) ◽  
pp. 18024-18043 ◽  
Author(s):  
Luiza M. Bessa ◽  
Hélène Launay ◽  
Marie Dujardin ◽  
François-Xavier Cantrelle ◽  
Guy Lippens ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Rna Polymerase ◽  
Hepatitis C Virus Rna ◽  
Intrinsically Disordered ◽  
Ns5a Protein ◽  
Virus Rna ◽  
Allosteric Regulator ◽  
Intrinsically Disordered Domain

scholarly journals Intrinsically disordered domain of kinesin-3 Kif14 enables unique functional diversity

2020 ◽  
Author(s):  
Ilia Zhernov ◽  
Stefan Diez ◽  
Marcus Braun ◽  
Zdenek Lansky
Keyword(s):  
Functional Diversity ◽  
Single Molecule ◽  
Mitotic Spindle ◽  
Cellular Functions ◽  
Protein Tau ◽  
Intrinsically Disordered ◽  
Order Of Magnitude ◽  
Pass Through ◽  
Domain I

ABSTRACTIn addition to their force-generating motor domains, kinesin motor proteins feature various accessory domains enabling them to fulfil a variety of functions in the cell. Human kinesin-3, Kif14, localizes to the midbody of the mitotic spindle and is involved in the progression of cytokinesis. The specific motor properties enabling Kif14’s cellular functions, however, remain unknown. Here, we show in vitro that it is the intrinsically disordered N-terminal domain of Kif14 that enables unique functional diversity of the motor. Using single molecule TIRF microscopy we observed that the presence of the disordered domain i) increased the Kif14 run-length by an order of magnitude, rendering the motor super-processive and enabling the motor to pass through highly crowded microtubule areas shielded by cohesive layers of microtubule-associated protein tau, which blocks less processive motors ii) enabled robust, autonomous Kif14 tracking of growing microtubule tips, independent of microtubule end-binding (EB) proteins and iii) enabled Kif14 to crosslink parallel microtubules and to drive the relative sliding of antiparallel ones. We explain these features of Kif14 by the observed increased affinity of the disordered domain for GTP-like tubulin and the observed diffusible interaction of the disordered domain with the microtubule lattice. We hypothesize that the disordered domain tethers the motor domain to the microtubule forming a diffusible foothold. We suggest that the intrinsically disordered N-terminal anchoring domain of Kif14 is a regulatory hub supporting the various cellular functions of Kif14 by tuning the motor’s interaction with microtubules.

scholarly journals A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication

2015 ◽  
Vol 290 (31) ◽  
pp. 19104-19120 ◽  
Author(s):  
Marie Dujardin ◽  
Vanesa Madan ◽  
Roland Montserret ◽  
Puneet Ahuja ◽  
Isabelle Huvent ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Rna Replication ◽  
Hepatitis C Virus Rna ◽  
Intrinsically Disordered ◽  
Ns5a Protein ◽  
Virus Rna ◽  
Intrinsically Disordered Domain

PPIP5K1 interacts with the exocyst complex through a C-terminal intrinsically disordered domain and regulates cell motility

2016 ◽  
Vol 28 (5) ◽  
pp. 401-411 ◽  
Author(s):  
Gayane Machkalyan ◽  
Phan Trieu ◽  
Darlaine Pétrin ◽  
Terence E. Hébert ◽  
Gregory J. Miller
Keyword(s):  
Cell Motility ◽  
Intrinsically Disordered ◽  
Exocyst Complex ◽  
Intrinsically Disordered Domain

scholarly journals Dissociation of the Dimer of the Intrinsically Disordered Domain of RNase Y upon Antibody Binding

2018 ◽  
Vol 115 (11) ◽  
pp. 2102-2113 ◽  
Author(s):  
Pierre Hardouin ◽  
Christophe Velours ◽  
Charles Bou-Nader ◽  
Nadine Assrir ◽  
Soumaya Laalami ◽  
...  
Keyword(s):  
Antibody Binding ◽  
Intrinsically Disordered ◽  
Rnase Y ◽  
Intrinsically Disordered Domain
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