The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

@article{Sternlicht1993TheTP,
  title={The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.},
  author={Himan Sternlicht and George W. Farr and M L Sternlicht and J Driscoll and Keith Willison and Michael B. Yaffe},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1993},
  volume={90 20},
  pages={
          9422-6
        }
}
A role in folding newly translated cytoskeletal proteins in the cytosol of eukaryotes has been proposed for t-complex polypeptide 1 (TCP1). In this study, we investigated tubulin and actin biogenesis in Chinese hamster ovary (CHO) cells. When extracts of pulse-labeled cells were analyzed by anion-exchange and size-exclusion chromatography, newly synthesized alpha-tubulin, beta-tubulin, and actin were observed to enter a large molecular mass complex (approximately 900 kDa). These proteins were… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 123 CITATIONS, ESTIMATED 58% COVERAGE

Knockdown of BmTCP-1β Delays BmNPV Infection in vitro

  • Front. Microbiol.
  • 2019
VIEW 2 EXCERPTS
CITES BACKGROUND

FILTER CITATIONS BY YEAR

1994
2019

CITATION STATISTICS

  • 3 Highly Influenced Citations

  • Averaged 6 Citations per year from 2017 through 2019