Journal
CURRENT BIOLOGY
Volume 21, Issue 7, Pages 586-591Publisher
CELL PRESS
DOI: 10.1016/j.cub.2011.02.046
Keywords
-
Categories
Funding
- National Institutes of Health [GM25661]
- National Natural Science Foundation of China [30830057, 30988004, 30771084]
- 973 program [2007CB914401]
- Specialized Research Fund for the Doctoral Program of Higher Education
Ask authors/readers for more resources
Flagella and cilia are structurally polarized organelles whose lengths are precisely defined, and alterations in length are related to several human disorders [1, 2]. Intraflagellar transport (IFT) and protein signaling molecules are implicated in specifying flagellar and ciliary length [3-6], but evidence has been lacking for a flagellum and cilium length sensor that could participate in active length control or establishment of structural polarity. Previously, we showed that the phosphorylation state of the aurora-like protein kinase CALK in Chlamydomonas is a marker of the absence of flagella. Here we show that CALK phosphorylation state is also a marker for flagellar length. CALK is phosphorylated in cells without flagella, and during flagellar assembly it becomes dephosphorylated. Dephosphorylation is not simply a consequence of initiation of flagellar assembly or of time after experimentally induced flagellar loss, but instead requires flagella to be assembled to a threshold length. Analysis of cells with flagella of varying lengths shows that the threshold length for CALK dephosphorylation is similar to 6 mu m (half length). Studies with short and long flagellar mutants indicate that cells detect absolute rather than relative flagellar length. Our results demonstrate that cells possess a mechanism for translating flagellar length into a posttranslational modification of a known flagellar regulatory protein.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available