Stopped in its tracks: Negative regulation of the dynein motor by the yeast protein She1

Moore, Jeffrey K.

doi:10.1002/bies.201300016

Cited by 3 publications

(3 citation statements)

References 53 publications

(106 reference statements)

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“…Processive movement was only observed after addition of the dynein‐1 processivity factor dynactin and a cargo adapter such as Bicaudal‐D , suggesting that cargo binding is able to directly regulate motor activity in some dyneins. There are also other regulator proteins known like Klarsicht , Halo and the S. cerevisiae dynein‐1 specific She1 . However, the best‐characterized dynein regulator is lissencephaly‐1 (Lis‐1).…”

Section: Introductionmentioning

confidence: 99%

Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement

Schmidt

2015

BioEssays

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Dyneins are a family of motor proteins that move along the microtubule. Motility is generated in the motor domain, which consists of a ring of six AAA+ (ATPases associated with diverse cellular activities) domains, the linker and the microtubule-binding domain (MTBD). The cyclic ATP-hydrolysis in the AAA+ ring causes the remodelling of the linker, which creates the necessary force for movement. The production of force has to be synchronized with cycles of microtubule detachment and rebinding to efficiently create movement along the microtubule. The analysis of four dynein motor domain crystal structures in the essay presented here provides evidence that this crucial coordination is carried out by open/closed AAA+ ring conformations.

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Section: Introductionmentioning

confidence: 99%

Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement

Schmidt

2015

BioEssays

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“…The nuclear movement in yeast remains restricted to the mother-bud as the septin ring is located at the junction between mother-and daughter-buds, whereas in hyphae, the nucleus travels through the germ tube (daughter-bud) [3,5]. During yeast mitosis through the budding process, spatiotemporal characteristics of mechanical interactions among various molecular players are likely to differ between mother-and daughter-buds [8,54,68,93]. For hyphae, the pattern of the interactions is unclear.…”

Section: Discussionmentioning

confidence: 99%

“…), remain off till the nucleus reaches the septin ring [67,68,[91][92][93]. In our simulation, we apply this mechanism and show the results in Fig.…”

Section: And ⃗ F Pull(h) Dynmentioning

confidence: 96%

A mechanistic model for nuclear migration in hyphae during mitosis

Som

Paul

2023

Preprint

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S. Cerevisiae and C. Albicans, the two well-known human pathogens, can be found in all three morphologies, i.e., yeast, pseudo-hyphae and true-hyphae. The cylindrical daughter-bud (germ tube) grows very long for true-hyphae, and the cell cycle is delayed compared to the other two morphologies. The place of the nuclear division is specific for true-hyphae determined by the position of the septin ring. However, the septin ring can localize anywhere inside the germ tube, unlike the mother-bud junction in budding yeast. Since the nucleus often migrates a long path in the hyphae, the underlying mechanism must be robust for executing mitosis in a timely manner. We explore the mechanism of nuclear migration through hyphae in light of mechanical interactions between astral microtubules and the cell cortex. We report that proper migration through constricted hyphae requires a large dynein pull applied on the astral microtubules from the hyphal cortex. This is achieved when the microtubules frequently slide along the hyphal cortex so that a large population of dyneins actively participate, pulling on them. Simulation shows timely migration when the dyneins from the mother cortex do not participate in pulling on the microtubules. These findings are robust for long migration and positioning of the nucleus in the germ tube at the septin ring.

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Mechanistic model for nuclear migration in hyphae during mitosis

Som

Paul

2023

Phys. Rev. E

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Stopped in its tracks: Negative regulation of the dynein motor by the yeast protein She1

Cited by 3 publications

References 53 publications

Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement

Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement

A mechanistic model for nuclear migration in hyphae during mitosis

Mechanistic model for nuclear migration in hyphae during mitosis

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