주광식 (KAIST) | 한빛사논문 > 한빛사

한빛사논문

조회4,418

KAIST

Proc. Natl. Acad. Sci. USA, April 9, 2013 vol. 110 no. 15 5987-5992. Published online before print March 25, 2013, doi: 10.1073/pnas.1220927110 CCDC41 is required for ciliary vesicle docking to the mother centriole

Abstract

Kwangsic Joo^a,1, Chang Gun Kim^a,1, Mi-Sun Lee^b, Hyun-Yi Moon^b, Sang-Hee Lee^a, Mi Jeong Kim^c, Hee-Seok Kweon^c, Woong-Yang Park^d,e, Cheol-Hee Kim^b,2, Joseph G. Gleeson^f,g,2, and Joon Kim^a,2

^aGraduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea;
^bDepartment of Biology, Chungnam National University, Daejeon 305-764, Korea;
^cDivision of Electron Microscopic Research, Korea Basic Science Institute, Daejeon 305-806, Korea;
^dSamsung Genome Institute, Samsung Medical Center, Seoul 135-710, Korea;
^eDepartment of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea; and
^fHoward Hughes Medical Institute, and
^gDepartment of Neurosciences, University of California at San Diego, La Jolla, CA 92093

Edited by Kathryn V. Anderson, Sloan?Kettering Institute, New York, NY, and approved March 4, 2013 (received for review December 4, 2012)

Abstract
The initiation of primary cilium assembly entails the docking of ciliary vesicles presumably derived from the Golgi complex to the distal end of the mother centriole. Distal appendages, which anchor the mother centriole to the plasma membrane, are thought to be involved in the docking process. However, little is known about the molecular players and mechanisms that mediate the vesicle?centriole association. Here we report that coiled-coil domain containing 41 (CCDC41) is required for the docking of ciliary vesicles. CCDC41 specifically localizes to the distal end of the mother centriole and interacts with centrosomal protein 164 (Cep164), a distal appendage component. In addition, a pool of CCDC41 colocalizes with intraflagellar transport protein 20 (IFT20) subunit of the intraflagellar transport particle at the Golgi complex. Remarkably, knockdown of CCDC41 inhibits the recruitment of IFT20 to the centrosome. Moreover, depletion of CCDC41 or IFT20 inhibits ciliogenesis at the ciliary vesicle docking step, whereas intraflagellar transport protein 88 (IFT88) depletion interferes with later cilium elongation steps. Our results suggest that CCDC41 collaborates with IFT20 to support the vesicle?centriole association at the onset of ciliogenesis.

ciliopathy, axoneme

¹K.J. and C.G.K. contributed equally to this work
²To whom correspondence may be addressed.

Author contributions: C.-H.K., J.G.G., and J.K. designed research; K.J., C.G.K., M.-S.L., H.-Y.M., S.-H.L., and M.J.K. performed research; K.J., H.-S.K., W.-Y.P., C.-H.K., and J.K. analyzed data; and J.K. wrote the paper.

논문정보

형식Research article
게재일2013년 03월 (BRIC 등록일 )
연구진국내(교신)+국외 연구진
분야 의약학 > 분자세포의학

댓글 작성 로그인

CV 열람하기

연락처 보기