期刊
MOLECULAR BIOLOGY OF THE CELL
卷 26, 期 15, 页码 2810-2822出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E15-03-0182
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资金
- Japan Society for the Promotion of Science [23657046, 24370079, 23570189]
- Uehara Memorial Foundation Research Fellowship for Research Abroad
- National Institutes of Health grant [GM30626]
- Robert W. Booth Endowment at the University of Massachusetts Medical School
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM030626, R01GM030626] Funding Source: NIH RePORTER
Ciliary length control is an incompletely understood process essential for normal ciliary function. The flagella of Chlamydomonas mutants lacking multiple axonemal dyneins are shorter than normal; previously it was shown that this shortness can be suppressed by the mutation suppressor of shortness 1 (ssh1) via an unknown mechanism. To elucidate this mechanism, we carried out genetic analysis of ssh1 and found that it is a new allele of TPG2 (hereafter tpg2-3), which encodes FAP234 functioning in tubulin polyglutamylation in the axoneme. Similar to the polyglutamylation-deficient mutants tpg1 and tpg2-1, tpg2-3 axonemal tubulin has a greatly reduced level of long polyglutamate side chains. We found that tpg1 and tpg2-1 mutations also promote flagellar elongation in short-flagella mutants, consistent with a polyglutamylation-dependent mechanism of suppression. Double mutants of tpg1 or tpg2-1 and fla10-1, a temperature-sensitive mutant of intraflagellar transport, underwent slower flagellar shortening than fla10-1 at restrictive temperatures, indicating that the rate of tubulin disassembly is decreased in the polyglutamylation-deficient flagella. Moreover, alpha-tubulin incorporation into the flagellar tips in temporary dikaryons was retarded in polyglutamylation-deficient flagella. These results show that polyglutamylation deficiency stabilizes axonemal microtubules, decelerating axonemal disassembly at the flagellar tip and shifting the axonemal assembly/disassembly balance toward assembly.
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