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Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex.

Publication ,  Journal Article
Williams, JC; Roulhac, PL; Roy, AG; Vallee, RB; Fitzgerald, MC; Hendrickson, WA
Published in: Proceedings of the National Academy of Sciences of the United States of America
June 2007

Cytoplasmic dynein is a microtubule-based motor protein complex that plays important roles in a wide range of fundamental cellular processes, including vesicular transport, mitosis, and cell migration. A single major form of cytoplasmic dynein associates with membranous organelles, mitotic kinetochores, the mitotic and migratory cell cortex, centrosomes, and mRNA complexes. The ability of cytoplasmic dynein to recognize such diverse forms of cargo is thought to be associated with its several accessory subunits, which reside at the base of the molecule. The dynein light chains (LCs) LC8 and TcTex1 form a subcomplex with dynein intermediate chains, and they also interact with numerous protein and ribonucleoprotein partners. This observation has led to the hypothesis that these subunits serve to tether cargo to the dynein motor. Here, we present the structure and a thermodynamic analysis of a complex of LC8 and TcTex1 associated with their intermediate chain scaffold. The intermediate chains effectively block the major putative cargo binding sites within the light chains. These data suggest that, in the dynein complex, the LCs do not bind cargo, in apparent disagreement with a role for LCs in dynein cargo binding interactions.

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Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

June 2007

Volume

104

Issue

24

Start / End Page

10028 / 10033

Related Subject Headings

  • X-Ray Diffraction
  • Thermodynamics
  • Static Electricity
  • Spectrum Analysis, Raman
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Binding
  • Molecular Sequence Data
  • Models, Molecular
  • Models, Biological
 

Citation

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Williams, J. C., Roulhac, P. L., Roy, A. G., Vallee, R. B., Fitzgerald, M. C., & Hendrickson, W. A. (2007). Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex. Proceedings of the National Academy of Sciences of the United States of America, 104(24), 10028–10033. https://doi.org/10.1073/pnas.0703614104
Williams, John C., Petra L. Roulhac, Anindya G. Roy, Richard B. Vallee, Michael C. Fitzgerald, and Wayne A. Hendrickson. “Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex.Proceedings of the National Academy of Sciences of the United States of America 104, no. 24 (June 2007): 10028–33. https://doi.org/10.1073/pnas.0703614104.
Williams JC, Roulhac PL, Roy AG, Vallee RB, Fitzgerald MC, Hendrickson WA. Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex. Proceedings of the National Academy of Sciences of the United States of America. 2007 Jun;104(24):10028–33.
Williams, John C., et al. “Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex.Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 24, June 2007, pp. 10028–33. Epmc, doi:10.1073/pnas.0703614104.
Williams JC, Roulhac PL, Roy AG, Vallee RB, Fitzgerald MC, Hendrickson WA. Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex. Proceedings of the National Academy of Sciences of the United States of America. 2007 Jun;104(24):10028–10033.
Journal cover image

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

June 2007

Volume

104

Issue

24

Start / End Page

10028 / 10033

Related Subject Headings

  • X-Ray Diffraction
  • Thermodynamics
  • Static Electricity
  • Spectrum Analysis, Raman
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Binding
  • Molecular Sequence Data
  • Models, Molecular
  • Models, Biological