Traffic control: regulation of kinesin motors

  title={Traffic control: regulation of kinesin motors},
  author={Kristen J. Verhey and Jennetta W. Hammond},
  journal={Nature Reviews Molecular Cell Biology},
Kinesins are a family of molecular motors that use the energy of ATP hydrolysis to move along the surface of, or destabilize, microtubule filaments. Much progress has been made in understanding the mechanics and functions of the kinesin motors that play important parts in cell division, cell motility, intracellular trafficking and ciliary function. How kinesins are regulated in cells to ensure the temporal and spatial fidelity of their microtubule-based activities is less well understood… 

Kinesin assembly and movement in cells.

Recent studies on the three major families involved in intracellular transport (kinesin-1, kines in-2, and kinesIn-3) that have begun to bridge the gap in knowledge between the in vitro and in vivo behaviors of kinesin motors are discussed.

Emerging Insights into the Function of Kinesin-8 Proteins in Microtubule Length Regulation

This review focuses on recent advances in understanding of the structure and function of the Kinesin-8 motor domain, and the emerging contributions of the C-terminal tail of KinesIn-8 proteins to regulate motor activity and localization.

Mechanisms for regulation of plant kinesins.

Progresses and prospects in microtubule depolymerizing Kinesin-13

This review will discuss the depolymerizing mechanisms of Kinesin-13, and comparison and analysis of Kineine-13s biological functions and regulations in different model organisms.

Kinesin Assembly and Movement in Cells

Recent studies have increased the understanding of how kinesin subunits assemble to produce a functional motor, how kinein motors are affected by biochemical cues and obstacles present on cellular microtubules, and how multiple motors on a cargo surface can work collectively for increased force production and travel distance.

Microtubule-Based Transport and the Distribution, Tethering, and Organization of Organelles.

The generation of biochemically distinct microtubule subpopulations allows subsets of motors to recognize a given microtubules identity, allowing further organization within the cytoplasm.

The Molecular Basis for Kinesin Functional Specificity During Mitosis

The recently identified molecular mechanisms that explain how the control and functional specification of mitotic kinesins is achieved are discussed.



Kinesin superfamily motor proteins and intracellular transport

The mechanisms by which different kinesin recognize and bind to specific cargos, as well as how kinesins unload cargo and determine the direction of transport, have now been identified and open exciting new areas of kinesIn research.

Conversion of Unc104/KIF1A Kinesin into a Processive Motor After Dimerization

It is shown that Unc104/KIF1A can dimerize and move unidirectionally and processively with rapid velocities characteristic of transport in living cells and that regulation of motor dimerization may be used to control transport by this class of kinesins.

Differential Regulation of Dynein and Kinesin Motor Proteins by Tau

The differential modulation of dynein and kinesin motility suggests that MAPs can spatially regulate the balance of microtubule-dependent axonal transport.

Kinesin’s tail domain is an inhibitory regulator of the motor domain

Both ATPase and motility assays indicate that the tail does not prevent kinesin from binding to microtubules, but rather reduces the motor’s stepping rate.

Intraflagellar transport motors in cilia: moving along the cell's antenna

My perspective on IFT as a model system for studying motor-driven cargo transport is presented and it is hypothesized that several accessory kinesins confer cilia-specific functions by augmenting the action of the two core IFT motors, kinesin-2 and dynein 1b, which assemble the cilium foundation.

Microtubule cross-linking triggers the directional motility of kinesin-5

Eg5, the vertebrate kinesin-5, has two modes of motion: an adenosine triphosphate–dependent directional mode and a diffusive mode that does not require ATP hydrolysis, and single-molecule experiments are used to examine how the switching between these modes is controlled.