Kristen J. Verhey
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View article: Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation
Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation Open
Microtubules are cytoskeletal filaments that self-assemble from the protein tubulin, a heterodimer of α-tubulin and β-tubulin, and are important for cell mechanics, migration, and division. Much work has focused on how the nucleotide state…
View article: Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation
Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation Open
Microtubules are cytoskeletal filaments that self-assemble from the protein tubulin, a heterodimer of α-tubulin and β-tubulin, and are important for cell mechanics, migration, and division. Much work has focused on how the nucleotide state…
View article: Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation
Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation Open
Microtubules are cytoskeletal filaments that self-assemble from the protein tubulin, a heterodimer of α-tubulin and β-tubulin, and are important for cell mechanics, migration, and division. Much work has focused on how the nucleotide state…
View article: The Kinesin-3 KIF1A Functions as a Diligent Worker during Axonal Transport
The Kinesin-3 KIF1A Functions as a Diligent Worker during Axonal Transport Open
Long-distance intracellular transport is driven by motor proteins that walk along microtubule tracks. The fate of the motor protein after transport is unclear. Classically, motor proteins have been thought to function as Diligent Workers (…
View article: MATCAP1 preferentially binds an expanded tubulin conformation to generate detyrosinated and ΔC2 α-tubulin
MATCAP1 preferentially binds an expanded tubulin conformation to generate detyrosinated and ΔC2 α-tubulin Open
Microtubules are cytoskeletal filaments with critical roles in cell division, cell motility, intracellular trafficking, and cilium function. In cells, subsets of microtubules are selectively marked by posttranslational modifications (PTMs)…
View article: Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays
Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays Open
Microtubules play essential roles in numerous cellular processes. All microtubules are built from the protein tubulin, yet individual microtubules can differ spatially and temporally due to their tubulin isotype composition and post‐transl…
View article: Micron-scale protein transport along microtubules by kinesin-driven shepherding
Micron-scale protein transport along microtubules by kinesin-driven shepherding Open
Microtubule-based long-distance transport in eukaryotic cells typically involves the binding of cargo to motors such as highly processive kinesins for unidirectional transport. An open question is whether long-distance transport can occur …
View article: Multi-kinesin clusters impart mechanical stress that reveals mechanisms of microtubule breakage in cells
Multi-kinesin clusters impart mechanical stress that reveals mechanisms of microtubule breakage in cells Open
Microtubules are cytoskeletal filaments that provide structural support for numerous cellular processes. Despite their high rigidity, microtubules can be dramatically bent in cells and it is unknown how much force a microtubule can withsta…
View article: Poxvirus A51R Proteins Negatively Regulate Microtubule-Dependent Transport by Kinesin-1
Poxvirus A51R Proteins Negatively Regulate Microtubule-Dependent Transport by Kinesin-1 Open
Microtubule (MT)-dependent transport is a critical means of intracellular movement of cellular cargo by kinesin and dynein motors. MT-dependent transport is tightly regulated by cellular MT-associated proteins (MAPs) that directly bind to …
View article: The kinesin-3 KIF1C undergoes liquid-liquid phase separation for accumulation of specific transcripts at the cell periphery
The kinesin-3 KIF1C undergoes liquid-liquid phase separation for accumulation of specific transcripts at the cell periphery Open
View article: The HSV-1 pUL37 protein promotes cell invasion by regulating the kinesin-1 motor
The HSV-1 pUL37 protein promotes cell invasion by regulating the kinesin-1 motor Open
Neurotropic alphaherpesviruses, including herpes simplex virus type 1 (HSV-1), recruit microtubule motor proteins to invade cells. The incoming viral particle traffics to nuclei in a two-step process. First, the particle uses the dynein–dy…
View article: Dual and opposing roles for the kinesin-2 motor, KIF17, in Hedgehog-dependent cerebellar development
Dual and opposing roles for the kinesin-2 motor, KIF17, in Hedgehog-dependent cerebellar development Open
While the kinesin-2 motors KIF3A and KIF3B have essential roles in ciliogenesis and Hedgehog (HH) signal transduction, potential role(s) for another kinesin-2 motor, KIF17, in HH signaling have yet to be explored. Here, we investigated the…
View article: Motor protein Kif6 regulates cilia motility and polarity in brain ependymal cells
Motor protein Kif6 regulates cilia motility and polarity in brain ependymal cells Open
Motile cilia on ependymal cells that line brain ventricular walls beat in concert to generate a flow of laminar cerebrospinal fluid (CSF). Dyneins and kinesins are ATPase microtubule motor proteins that promote the rhythmic beating of cili…
View article: Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Author Response: Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Author Response: Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
View article: KIF1C, an RNA transporting kinesin-3, undergoes liquid-liquid phase separation through its C-terminal disordered domain
KIF1C, an RNA transporting kinesin-3, undergoes liquid-liquid phase separation through its C-terminal disordered domain Open
The spatial distribution of mRNA is critical for local control of protein production. Recent studies have identified the kinesin-3 family member KIF1C as an RNA transporter. However, it is not clear how KIF1C interacts with RNA molecules. …
View article: Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Reviewer #2 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Reviewer #2 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Author Response: Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Author Response: Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Reviewer #1 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Reviewer #1 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Microtubule detyrosination by VASH1/SVBP is regulated by the conformational state of tubulin in the lattice
Microtubule detyrosination by VASH1/SVBP is regulated by the conformational state of tubulin in the lattice Open
View article: Zn2+ decoration of microtubules arrests axonal transport and displaces tau, doublecortin, and MAP2C
Zn2+ decoration of microtubules arrests axonal transport and displaces tau, doublecortin, and MAP2C Open
Intracellular Zn2+ concentrations increase via depolarization-mediated influx or intracellular release, but the immediate effects of Zn2+ signals on neuron function are not fully understood. By simultaneous recording of cytosolic Zn2+ and …
View article: Temperature-dependent RNA editing in octopus extensively recodes the neural proteome
Temperature-dependent RNA editing in octopus extensively recodes the neural proteome Open
View article: Reviewer #2 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Reviewer #2 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Reviewer #1 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Reviewer #1 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Autoinhibited kinesin-1 adopts a hierarchical folding pattern
Autoinhibited kinesin-1 adopts a hierarchical folding pattern Open
Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited…
View article: Causes, costs and consequences of kinesin motors communicating through the microtubule lattice
Causes, costs and consequences of kinesin motors communicating through the microtubule lattice Open
Microtubules are critical for a variety of important functions in eukaryotic cells. During intracellular trafficking, molecular motor proteins of the kinesin superfamily drive the transport of cellular cargoes by stepping processively alon…
View article: Kif6 regulates cilia motility and polarity in brain ependymal cells
Kif6 regulates cilia motility and polarity in brain ependymal cells Open
Ependymal cells, lining brain ventricular walls, display tufts of cilia that beat in concert promoting laminar Cerebrospinal fluid (CSF) flow within brain ventricles. The ciliary axonemes of multiciliated ependymal cells display a 9+2 micr…
View article: Mechanistic Analysis of CCP1 in Generating ΔC2 α-Tubulin in Mammalian Cells and Photoreceptor Neurons
Mechanistic Analysis of CCP1 in Generating ΔC2 α-Tubulin in Mammalian Cells and Photoreceptor Neurons Open
An important post-translational modification (PTM) of α-tubulin is the removal of amino acids from its C-terminus. Removal of the C-terminal tyrosine residue yields detyrosinated α-tubulin, and subsequent removal of the penultimate glutama…