Dynein

Cytoplasmic dynein carries cargo along microtubules toward the ?blank.

Alone, human dynein-1 is mostly inactive. Which two partners switch it on?

What forms the ring at the core of each dynein motor domain?

Which of dynein's six AAA+ domains is the main site that splits ATP?

Dynein's ATPase ring reaches the microtubule through a coiled-coil ?blank about 15 nm long, with the microtubule-binding foot (MTBD) at its tip.

The most frequent step of yeast dynein is ?blank, close to the spacing of tubulin dimers.

How did Can and colleagues make yeast dynein walk toward the plus end?

When ATP binds AAA1, dynein's ring of six AAA+ domains ?blank.

Dynein's stalk carries the signal from the ring to the foot by helix ?blank, not by bending.

In dynein's stalk, what does the registry (the alignment) of the two helices CC1 and CC2 control?

After ATP binds, why is dynein's linker forced into a bent, primed shape?

When dynein's primed head rebinds the microtubule, phosphate leaves and the linker ?blank: this is the power stroke.

Which step of the dynein cycle appears to be the slow one?

Dynein's two heads step mostly independently, but they show coordination when far apart. What kind of mechanism does that point to?

In the classic dynein cycle, the head rebinds the microtubule before its linker straightens. What did Chai and colleagues see that does not fit this order?

Dynein-driven cilia line your airways. What do they push up toward your throat?

An adult human lung holds an estimated ?blank motile cilia, each driven by dynein.

Dynein arms try to slide one rail of a cilium's axoneme past the next. Why does the cilium bend instead?

In primary ciliary dyskinesia, airway cilia lack their dynein arms. What happens to the mucus?

A cilium is like a bimetal strip: two tied layers turn a change in length into a bend. Where does that analogy break down?

By calculation, about how many outer dynein arms does one airway cilium hold?

How did Reck-Peterson and colleagues measure the 8 nm step of yeast dynein?

A label on one head of yeast dynein moved about 16 to 18 nm per step, twice as far as the tail's 8 nm. Why?

Pulled backward with more than its stall force, yeast dynein walks ?blank.

Reported stall forces for full-length yeast dynein differ about ?blank: 7 pN (Gennerich 2007) versus 3.6 pN (Belyy 2016).

How did Belyy and colleagues make their optical trap pull only on complete dynein–dynactin–BICD2 complexes?

One dynein–dynactin–BICD2 complex was linked to one kinesin-1. How did the pair move?

Why do dynein complexes built with the adaptors BICDR1 or HOOK3 pull harder and move faster than those built with BICD2?