Regulation of microtubule stability and organization by mammalian Par3 in specifying neuronal polarity. Chen, S., Chen, J., Shi, H., Wei, M., Castaneda-Castellanos, D. R, Bultje, R. S, Pei, X., Kriegstein, A. R, Zhang, M., & Shi, S. Dev Cell, 24(1):26–40, December, 2012.
abstract   bibtex   
Polarization of mammalian neurons with a specified axon requires precise regulation of microtubule and actin dynamics in the developing neurites. Here we show that mammalian partition defective 3 (mPar3), a key component of the Par polarity complex that regulates the polarization of many cell types including neurons, directly regulates microtubule stability and organization. The N-terminal portion of mPar3 exhibits strong microtubule binding, bundling, and stabilization activity, which can be suppressed by its C-terminal portion via an intramolecular interaction. Interestingly, the intermolecular oligomerization of mPar3 is able to relieve the intramolecular interaction and thereby promote microtubule bundling and stabilization. Furthermore, disruption of this microtubule regulatory activity of mPar3 impairs its function in axon specification. Together, these results demonstrate a role for mPar3 in directly regulating microtubule organization that is crucial for neuronal polarization.
@ARTICLE{Chen2012-yi,
  title    = "Regulation of microtubule stability and organization by mammalian
              Par3 in specifying neuronal polarity",
  author   = "Chen, She and Chen, Jia and Shi, Hang and Wei, Michelle and
              Castaneda-Castellanos, David R and Bultje, Ronald S and Pei, Xin
              and Kriegstein, Arnold R and Zhang, Mingjie and Shi, Song-Hai",
  abstract = "Polarization of mammalian neurons with a specified axon requires
              precise regulation of microtubule and actin dynamics in the
              developing neurites. Here we show that mammalian partition
              defective 3 (mPar3), a key component of the Par polarity complex
              that regulates the polarization of many cell types including
              neurons, directly regulates microtubule stability and
              organization. The N-terminal portion of mPar3 exhibits strong
              microtubule binding, bundling, and stabilization activity, which
              can be suppressed by its C-terminal portion via an intramolecular
              interaction. Interestingly, the intermolecular oligomerization of
              mPar3 is able to relieve the intramolecular interaction and
              thereby promote microtubule bundling and stabilization.
              Furthermore, disruption of this microtubule regulatory activity
              of mPar3 impairs its function in axon specification. Together,
              these results demonstrate a role for mPar3 in directly regulating
              microtubule organization that is crucial for neuronal
              polarization.",
  journal  = "Dev Cell",
  volume   =  24,
  number   =  1,
  pages    = "26--40",
  month    =  dec,
  year     =  2012,
  language = "en"
}

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