TY - JOUR
T1 - The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility
AU - Yamamoto, Ryosuke
AU - Song, Kangkang
AU - Yanagisawa, Haru aki
AU - Fox, Laura
AU - Yagi, Toshiki
AU - Wirschell, Maureen
AU - Hirono, Masafumi
AU - Kamiya, Ritsu
AU - Nicastro, Daniela
AU - Sale, Winfield S.
PY - 2013/4/15
Y1 - 2013/4/15
N2 - 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.
AB - 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.
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U2 - 10.1083/jcb.201211048
DO - 10.1083/jcb.201211048
M3 - Article
C2 - 23569216
AN - SCOPUS:84876716007
SN - 0021-9525
VL - 201
SP - 263
EP - 278
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 2
ER -