Dynactin Enhances the Processivity of Kinesin‐2

  title={Dynactin Enhances the Processivity of Kinesin‐2},
  author={Matthew A Berezuk and Trina A. Schroer},
Kinesin‐2 is a major microtubule‐based motor in most cell types. Its in vitro motile properties have been analyzed extensively and been found to differ considerably from kinesin‐1. Although recombinant kinesin‐2 heterodimers exhibit processive movement, the processivity of the native kinesin‐2 holoenzyme has never been evaluated. Kinesin‐2 can interact with dynactin, a ‘processivity factor’ for cytoplasmic dynein, which may alter its motile properties. In this study, we analyze the in vitro… 

Function and regulation of kinesin-1, -2 and -3

This work presents the first evidence that kinesin-1-driven ER movement, and not simply network morphology, varies during cell division, which is postulated to contribute to the well documented changes in organelle positioning and cargo transit through membrane trafficking pathways which occur duringcell division.

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.

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.

Myosin V and Kinesin act as tethers to enhance each others' processivity

It is shown, using single-molecule techniques, that a functional consequence of myosin V's diffusion on microtubules is a significant enhancement of the processive run length of kinesin when both motors are present on the same cargo.

Partial Characterization of an Interaction between Kinesin Associated Protein 3 (Kap3) of Kinesin-2 and the Actin Cytoskeleton

It is reported that KAP3 associates with actin polymers exclusively through its central core of armadillo repeats, providing further insight into how KAB3 facilitates kinesin-2 transport activities, specifically those related to the formation and maintenance of specific cellular processes and cell shape.

Kinesin-2: a family of heterotrimeric and homodimeric motors with diverse intracellular transport functions.

  • J. Scholey
  • Biology
    Annual review of cell and developmental biology
  • 2013
Functional studies suggest that cooperation between different types of kinesin-2 motors or between kines in-2 and a member of a different motor family can generate diverse patterns of anterograde intracellular transport.

Regulation of processive motion and microtubule localization of cytoplasmic dynein.

An overview of dynein's motile properties is given, with a special emphasis on processivity and its regulation, and recent findings of different pathways for microtubule plus-end loading of dyNEin are summarized.

Distinct retrograde microtubule motor sets drive early and late endosome transport

Evidence is provided that distinct minus end‐directed MT motor systems drive the differential transport and subcellular distribution of EEs and LEs in mammalian cells.



Dynactin is required for bidirectional organelle transport

Dynactin is required for transport activity of microtubule motors of opposite polarity, cytoplasmic dynein and kinesin II, and may provide a new mechanism to coordinate their activities, as revealed in Xenopus laevis melanophores.

Single-molecule behavior of monomeric and heteromeric kinesins.

The results suggest that these motors have low duty cycles and that high processivity may not be required for efficient vesicle transport, and conventional kinesin's unusual processivity might not be necessary for efficient transport of protein complexes that cannot carry multiple motors.

Dynactin increases the processivity of the cytoplasmic dynein motor

The results indicate that dynactin acts as a processivity factor for cytoplasmic-dynein-based motility and provide the first evidence that cytoskeletal motor processivity can be affected by extrinsic factors.

Kinesin‐2 is a Motor for Late Endosomes and Lysosomes

Despite the abnormal subcellular distribution of late endosomes/lysosomes, the uptake and trafficking of molecules through the conventional endocytic pathway appeared to be unaffected, and the slow time–course of inhibition suggests that both kinesin‐2 itself and its attachment to membranes do not turn over quickly.

Fractionation and Characterization of Kinesin II Species in Vertebrate Brain

This work isolated nucleotide‐dependent, microtubule‐binding proteins from 13‐day chick embryo brain and identified three KIF species, the most abundant species, kinesin I, which exhibited the expected long range micro tubule gliding activity, and KIF1C, which did not move microtubules.

Coordination between Motor Domains in Processive Kinesins*

The phenomenon of kinesin processivity is reviewed from a complementary perspective by considering specific structural features of the motor domains that underlie their coordination, and how these features contribute to its processive movement.

A processive single-headed motor: kinesin superfamily protein KIF1A.

A motor-domain construct of KIF1A, a single-headed kinesin superfamily protein, was shown to move processively along the microtubule for more than 1 micrometer and fitted a biased Brownian-movement model.

Understanding the functions of kinesin-II.