Dissect Kif5b in nuclear positioning during myogenesis: The light chain binding domain and the autoinhibitory peptide are both indispensable

Zai Wang, Wenqian Xue, Xiuling Li, Raozhou Lin, Ju Cui, Jian Dong Huang

Research output: Contribution to journalArticlepeer-review

Abstract

The microtubule motor kinesin-1 is responsible for the nuclear positioning during myogenesis. Here we show that the coiled-coil stalk/tail domain containing the kinesin light chain (KLC) binding sites targets to the perinuclear region like endogenous Kif5b, while the globular tail domain cannot. To investigate which fragments of kinesin heavy chain (Kif5b) is responsible for the myonuclear positioning, we transfect Kif5b expression constructs into Kif5b deficient myoblasts and test their ability to rescue the myonuclear phenotype. We find that the KLC binding domain and the autoinhibitory peptide in the globular tail region are both indispensable for the nuclear membrane localization of Kif5b and the kinesin-1-mediated myonuclear positioning. These results suggest that while the KLC binding domain may directly targets Kif5b to the myonuclear membrane, the autoinhibitory peptide may play an indirect role in regulating the kinesin-1-mediated myonuclear positioning.

Original languageEnglish (US)
Pages (from-to)242-247
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume432
Issue number2
DOIs
StatePublished - Mar 8 2013
Externally publishedYes

Keywords

  • Autoinhibitory peptide
  • KLC binding domain
  • Kif5b
  • Myonuclear positioning
  • Nesprin 4

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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