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IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding

  • Maureen Wirschell
  • , Chun Yang
  • , Pinfen Yang
  • , Laura Fox
  • , Haru Aki Yanagisawa
  • , Ritsu Kamiya
  • , George B. Witman
  • , Mary E. Porter
  • , Winfield S. Sale

Research output: Contribution to journal › Article › peer-review

Abstract

Our goal is to understand the assembly and regulation of flagellar dyneins, particularly the Chlamydomonas inner arm dynein called I1 dynein. Here, we focus on the uncharacterized I1-dynein IC IC97. The IC97 gene encodes a novel IC without notable structural domains. IC97 shares homology with the murine lung adenoma susceptibility 1 (Las1) protein - a candidate tumor suppressor gene implicated in lung tumorigenesis. Multiple, independent biochemical assays determined that IC97 interacts with both α- and β-tubulin subunits within the axoneme. I1-dynein assembly mutants suggest that IC97 interacts with both the IC138 and IC140 subunits within the I1-dynein motor complex and that IC97 is part of a regulatory complex that contains IC138. Microtubule sliding assays, using axonemes containing I1 dynein but devoid of IC97, show reduced microtubule sliding velocities that are not rescued by kinase inhibitors, revealing a critical role for IC97 in I1-dynein function and control of dynein-driven motility.

Original languageEnglish (US)
Pages (from-to)3044-3054
Number of pages11
JournalMolecular Biology of the Cell
Volume20
Issue number13
DOIs
StatePublished - Jul 1 2009

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