The 29 kDa light chain that regulates axonemal dynein activity binds to cytoplasmic dyneins

Hali Wang, Peter Satir

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

In earlier studies, Hamasaki et al. (Proc. Natl. Acad. USA. 88:7918- 7922, 1991) and Barkalow et al. (J. Cell Biol. 126:727-735, 1994) found that cAMP- and Ca2+-sensitive phosphorylation of a 29 kDa dynein light chain (p29) extracted from 22S axonemal dynein of Paramecium, regulates the velocity of in vitro microtubule translocation and ciliate swimming speed. In this study we report evidence of recombination of p29 to cytoplasmic dyneins from both rat liver and Paramecium, as well as to 22S dynein precursor molecule, based on immunoprecipitation and force filtration data. Immunoprecipitation also provides additional evidence for the binding of p29 to 22S axonemal dynein. The results suggest that p29 might regulate cytoplasmic dynein, as well as axonemal dynein function in Paramecium, and that a homologue of 29 may exist in rat liver and other mammalian cells.

Original languageEnglish (US)
Pages (from-to)1-8
Number of pages8
JournalCell motility and the cytoskeleton
Volume39
Issue number1
DOIs
StatePublished - Jan 31 1998

Keywords

  • Axoneme
  • Cytoplasmic dynein
  • Paramecium
  • Rat liter
  • Regulatory light chain

ASJC Scopus subject areas

  • Structural Biology
  • Cell Biology

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