Author response: Cytoplasmic dynein crosslinks and slides anti-parallel microtubules using its two motor domains
Year: 2013
Type: peer-review
Abstract: When cells divide, they must also divide their contents. In particular, both ‘mother’ and ‘daughter’ cells require full sets of chromosomes, which must first be duplicated, and then evenly distributed between the cells. Protein filaments called microtubules form a network that helps to accurately segregate the chromosomes. Microtubules emanate from structures at each end of the dividing cell known as spindle poles; after the chromosomes have duplicated, the microtubules latch onto them and align the pairs in the middle of the cell. As the two cells separate, microtubules at opposite spindle poles reel in one chromosome from each pair. Microtubules are composed of alternating copies of two different types of a protein called tubulin, and have ends with distinct properties. The ‘minus’ ends are directed outwards, away from the chromosomes; the ‘plus’ ends—which can actively add tubulin—grow toward the middle of the cell, and can also bind to chromosomes. Microtubules can be manipulated by motor proteins that ‘walk’ along them carrying cargoes, which can include other microtubules. The combined actions of many motor proteins rearrange the microtubule network into a configuration that enables the chromosomes, and other cellular structures, to partition equally between the mother and daughter cells. Motor proteins such as dynein and kinesin transport cargoes along microtubules; each motor is composed of two identical copies of the protein bound to each other. Kinesin walks toward the plus end of a microtubule, propelling itself using ‘feet’ that are called motor domains; it binds cargoes (including other microtubules) through additional regions located at the opposite end of the protein. In contrast, dynein walks toward the minus end of a microtubule. Although dynein is known to carry certain cargoes through regions outside its motor domain, how it transports other microtubules is not well understood. Tanenbaum et al. now show that regions outside the motor domain of dynein are unnecessary to transport microtubule cargoes. When two dynein motor domains are isolated and linked to each other in vitro, each can bind to a separate microtubule. By walking toward the minus ends of their respective microtubules, the motor domains drive the microtubules in opposite directions, sliding them apart. These studies thus provide insight into the mechanism through which dynein works with additional motor proteins (such as kinesin) to rearrange microtubules during cell division—and also to ensure that chromosomes segregate evenly between mother and daughter cells.
Source: eLife
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,500
OpenAlex ID: W2988927585