May 2008
Volume 49, Issue 13
ARVO Annual Meeting Abstract  |   May 2008
Dynamic Regulation of Microtubule Assembly by the Shsp and Molecular Chaperone, Human B Crystallin
Author Affiliations & Notes
  • J. I. Clark
    University of Washington, Seattle, Washington
    Biological Structure and Ophthalmology,
  • S. Haouck
    University of Washington, Seattle, Washington
    Biological Structure,
  • J. Ghosh
    Laboratory of Molecular Aging, Harvard Medical School, Boston, Massachusetts
  • Footnotes
    Commercial Relationships  J.I. Clark, None; S. Haouck, None; J. Ghosh, None.
  • Footnotes
    Support  EY04542
Investigative Ophthalmology & Visual Science May 2008, Vol.49, 3800. doi:
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      J. I. Clark, S. Haouck, J. Ghosh; Dynamic Regulation of Microtubule Assembly by the Shsp and Molecular Chaperone, Human B Crystallin. Invest. Ophthalmol. Vis. Sci. 2008;49(13):3800. doi:

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      © ARVO (1962-2015); The Authors (2016-present)

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Purpose: : To evaluate the function of interactive sequences in human αB crystallin on dynamic subunit exchange and microtubule assembly.

Methods: : Five interactive sequences in αB crystallin were synthesized as individual peptides for experimental studies on the assembly of microtubules in vitro using a fluorescence DAPI assay (Ghosh et al. 2007 PloS one 6:3498). Mutations at corresponding positions in full-length αB crystallin were used experimentally to confirm the importance of these interactive sequences in the αB crystallin:tubulin interaction.

Results: : αB crystallin inhibited microtubule assembly at molar ratios >2:1, αB crystallin:tubulin and promoted microtubule assembly at molar ratios between 1:4 and 2:1. The plot of assembly versus molar ratio was parabolic with a maximum at approximately 0.5:1 αB:tubulin. The synthetic peptide corresponding to the αB crystallin interactive sequence, 113FISREFHR120, in the β3 strand of the α-crystallin core domain partially inhibited microtubule assembly. In contrast, the peptides 131LTITSSLSSDGV142 in the β8 strand and loop region of the core domain and 156ERTIPITRE164 in the C-terminal extension promoted microtubule assembly. Mutations in these exposed interactive sequences in full-length αB crystallin altered interactions with microtubules.

Keywords: crystallins • cataract • protein structure/function 

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