Authors
Yang, PinfenDiener, Dennis R.
Yang, Chun
Kohno, Takahiro
Pazour, Gregory J.
Dienes, Jennifer M.
Agrin, Nathan S.
King, Stephen M.
Sale, Winfield S.
Kamiya, Ritsu
Rosenbaum, Joel L.
Witman, George B.
Document Type
Journal ArticlePublication Date
2006-03-02Keywords
Amino Acid SequenceAnimals
Chlamydomonas
Electrophoresis, Gel, Two-Dimensional
Flagella
HSP40 Heat-Shock Proteins
Models, Molecular
Molecular Sequence Data
*Protozoan Proteins
Sequence Homology, Amino Acid
Cell Biology
Metadata
Show full item recordAbstract
The radial spoke is a ubiquitous component of '9+2' cilia and flagella, and plays an essential role in the control of dynein arm activity by relaying signals from the central pair of microtubules to the arms. The Chlamydomonas reinhardtii radial spoke contains at least 23 proteins, only 8 of which have been characterized at the molecular level. Here, we use mass spectrometry to identify 10 additional radial spoke proteins. Many of the newly identified proteins in the spoke stalk are predicted to contain domains associated with signal transduction, including Ca2+-, AKAP- and nucleotide-binding domains. This suggests that the spoke stalk is both a scaffold for signaling molecules and itself a transducer of signals. Moreover, in addition to the recently described HSP40 family member, a second spoke stalk protein is predicted to be a molecular chaperone, implying that there is a sophisticated mechanism for the assembly of this large complex. Among the 18 spoke proteins identified to date, at least 12 have apparent homologs in humans, indicating that the radial spoke has been conserved throughout evolution. The human genes encoding these proteins are candidates for causing primary ciliary dyskinesia, a severe inherited disease involving missing or defective axonemal structures, including the radial spokes.Source
J Cell Sci. 2006 Mar 15;119(Pt 6):1165-74. Epub 2006 Feb 28. Link to article on publisher's siteDOI
10.1242/jcs.02811Permanent Link to this Item
http://hdl.handle.net/20.500.14038/26533PubMed ID
16507594Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1242/jcs.02811