The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility

Ryosuke Yamamoto, Kangkang Song, Haru aki Yanagisawa, Laura Fox, Toshiki Yagi, Maureen Wirschell, Masafumi Hirono, Ritsu Kamiya, Daniela Nicastro, Winfield S. Sale

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MIA1 and MIA2 genes encode conserved coiled-coil proteins, FAP100 and FAP73, respectively, which form the modifier of inner arms (MIA) complex in flagella. Cryo-electron tomography of mia mutant axonemes revealed that the MIA complex was located immediately distal to the intermediate/light chain complex of I1 dynein and structurally appeared to connect with the nexin-dynein regulatory complex. In axonemes from mutants that lack both the outer dynein arms and the MIA complex, I1 dynein failed to assemble, suggesting physical interactions between these three axonemal complexes and a role for the MIA complex in the stable assembly of I1 dynein. The MIA complex appears to regulate I1 dynein and possibly outer arm dyneins, which are both essential for normal motility.

Original languageEnglish (US)
Pages (from-to)263-278
Number of pages16
JournalJournal of Cell Biology
Volume201
Issue number2
DOIs
StatePublished - Apr 15 2013

ASJC Scopus subject areas

  • Cell Biology

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