Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers.

@article{Wang2010Dynamin2M,
  title={Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers.},
  author={Lei Wang and Barbara Barylko and Christopher E. Byers and J. B. Alexander Ross and David Jameson and Joseph P Albanesi},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 30},
  pages={22753-7}
}
Mutations in the dynamin 2 gene have been identified in patients with autosomal dominant forms of centronuclear myopathy (CNM). Dynamin 2 is a ubiquitously expressed approximately 100-kDa GTPase that assembles around the necks of vesiculating membranes and promotes their constriction and scission. It has also been implicated in regulation of the actin and microtubule cytoskeletons. At present, the cellular functions of dynamin 2 that are affected by CNM-linked mutations are not well defined… CONTINUE READING

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It has also been implicated in regulation of the actin and microtubule cytoskeletons .
It has also been implicated in regulation of the actin and microtubule cytoskeletons .
Dynamin 2 is a ubiquitously expressed approximately 100-kDa GTPase that assembles around the necks of vesiculating membranes and promotes their constriction and scission .
All four mutants display higher than wild - type GTPase activities , and more importantly , the mutants form high order oligomers that are significantly more resistant than wild - type dynamin 2 to disassembly by guanine nucleotides or high ionic strength .
It has also been implicated in regulation of the actin and microtubule cytoskeletons .
It has also been implicated in regulation of the actin and microtubule cytoskeletons .
MicrotubulesConstitutional part ofCytoskeleton
It has also been implicated in regulation of the actin and microtubule cytoskeletons .
MicrotubulesAnatomic structure is physical part ofCytoskeleton
It has also been implicated in regulation of the actin and microtubule cytoskeletons .
All four mutants display higher than wild - type GTPase activities , and more importantly , the mutants form high order oligomers that are significantly more resistant than wild - type dynamin 2 to disassembly by guanine nucleotides or high ionic strength .
Dynamin 2 is a ubiquitously expressed approximately 100-kDa GTPase that assembles around the necks of vesiculating membranes and promotes their constriction and scission .
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