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Dnm1 forms spirals that are structurally tailored to fit mitochondria

Open access
Ingerman, Elena, Perkins, Edward M., Marino, Michael, Mears, Jason A., McCaffery, J. Michael, Hinshaw, Jenny E., Nunnari, Jodi·2005·The Journal of Cell Biology

Abstract

Dynamin-related proteins (DRPs) are large self-assembling GTPases whose common function is to regulate membrane dynamics in a variety of cellular processes. Dnm1, which is a yeast DRP (Drp1/Dlp1 in humans), is required for mitochondrial division, but its mechanism is unknown. We provide evidence that Dnm1 likely functions through self-assembly to drive the membrane constriction event that is associated with mitochondrial division. Two regulatory features of Dnm1 self-assembly were also identified. Dnm1 self-assembly proceeded through a rate-limiting nucleation step, and nucleotide hydrolysis by assembled Dnm1 structures was highly cooperative with respect to GTP. Dnm1 formed extended spirals, which possessed diameters greater than those of dynamin-1 spirals but whose sizes, remarkably, were equal to those of mitochondrial constriction sites in vivo. These data suggest that Dnm1 has evolved to form structures that fit the dimensions of mitochondria.

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Metadata

Authors
Ingerman, E., Perkins, E. M., Marino, M., Mears, J. A., McCaffery, J. M., Hinshaw, J. E., & Nunnari, J.
Venue
The Journal of Cell Biology
Published
2005-09-26
Volume
170
Issue
7
Pages
1021-1027
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2161892574
Cited by
575
References
2
FWCI
6.34
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Dnm1 forms spirals that are structurally tailored to fit mitochondria. https://app.cochat.ai/papers/10.1083/jcb.200506078
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Ingerman, E., Perkins, E. M., Marino, M., Mears, J. A., McCaffery, J. M., Hinshaw, J. E., & Nunnari, J. (2005). Dnm1 forms spirals that are structurally tailored to fit mitochondria. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200506078

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