Emerging mechanisms of dynein transport in the cytoplasm versus the cilium.

Anthony J Roberts

doi:10.1042/bst20170568

Abstract

Two classes of dynein power long-distance cargo transport in different cellular contexts. Cytoplasmic dynein-1 is responsible for the majority of transport toward microtubule minus ends in the cell interior. Dynein-2, also known as intraflagellar transport dynein, moves cargoes along the axoneme of eukaryotic cilia and flagella. Both dyneins operate as large ATP-driven motor complexes, whose dysfunction is associated with a group of human disorders. But how similar are their mechanisms of action and regulation? To examine this question, this review focuses on recent advances in dynein-1 and -2 research, and probes to what extent the emerging principles of dynein-1 transport could apply to or differ from those of the less well-understood dynein-2 mechanoenzyme.

Highlights

Dyneins are minus-end-directed microtubule motor proteins in eukaryotic cells, built around forcegenerating subunits termed ‘heavy chains’
Rather than involving small groups of motors bound to cargo via dynactin, dynein-2 transport occurs in the context of long linear intraflagellar transport (IFT) trains [33,34], which can contain dozens of motors [52] (Figure 1)
Its enzymatic core is a ring of six AAA+ (ATPases associated with various cellular activities) modules (AAA1–6) with an associated C-terminal domain (CTD) [95]

Summary

Introduction

Dyneins are minus-end-directed microtubule motor proteins in eukaryotic cells, built around forcegenerating subunits termed ‘heavy chains’. Two dyneins function as motors that transport cargo: cytoplasmic dynein-1 and -2 (Figure 1). Rather than involving small groups of motors bound to cargo via dynactin, dynein-2 transport occurs in the context of long linear IFT trains [33,34], which can contain dozens of motors [52] (Figure 1).

Results

Conclusion