Dynamics of the IFT machinery at the ciliary tip

被引：97

作者：

Chien, Alexander ^{[1
]}

Shih, Sheng Min ^{[2
]}

Bower, Raquel ^{[3
]}

Tritschler, Douglas ^{[3
]}

Porter, Mary E. ^{[3
]}

Yildiz, Ahmet ^{[1
,2
,4
]}

机构：

[1] Univ Calif Berkeley, Biophys Grad Grp, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Phys Dept, Berkeley, CA 94720 USA

[3] Univ Minnesota, Dept Genet Cell Biol & Dev, Minneapolis, MN USA

[4] Univ Calif Berkeley, Dept Mol & Cell Biol, 229 Stanley Hall, Berkeley, CA 94720 USA

来源：

ELIFE | 2017年 / 6卷

基金：

美国国家科学基金会;

关键词：

RETROGRADE INTRAFLAGELLAR TRANSPORT; LIGHT INTERMEDIATE CHAIN; FLAGELLAR LENGTH; CYTOPLASMIC DYNEIN; CHLAMYDOMONAS; PROTEINS; CARGO; MOTORS; CYCLE; CELL;

D O I：

10.7554/eLife.28606

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Intraflagellar transport (IFT) is essential for the elongation and maintenance of eukaryotic cilia and flagella. Due to the traffic jam of multiple trains at the ciliary tip, how IFT trains are remodeled in these turnaround zones cannot be determined by conventional imaging. Using PhotoGate, we visualized the full range of movement of single IFT trains and motors in Chlamydomonas flagella. Anterograde trains split apart and IFT complexes mix with each other at the tip to assemble retrograde trains. Dynein-1b is carried to the tip by kinesin-II as inactive cargo on anterograde trains. Unlike dynein-1b, kinesin-II detaches from IFT trains at the tip and diffuses in flagella. As the flagellum grows longer, diffusion delays return of kinesin-II to the basal body, depleting kinesin-II available for anterograde transport. Our results suggest that dissociation of kinesin-II from IFT trains serves as a negative feedback mechanism that facilitates flagellar length control in Chlamydomonas.

引用

页数：25

共 50 条

[1] Single-molecule dynein, kinesin and IFT particle dynamics at the C. elegans ciliary tip
Mijalkovic, J.
van Krugten, J.
Oswald, F.
Acar, S.
Peterman, E. J.
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2017, 46 : S365 - S365
[2] Single-molecule dynein, kinesin and IFT particle dynamics at the C. elegans ciliary tip
Mijalkovic, J.
van Krugten, J.
Oswald, F.
Acar, S.
Peterman, E. J.
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2017, 46 : S106 - S106
[3] Architecture of the IFT ciliary trafficking machinery and interplay between its components
Nakayama, Kazuhisa
Katoh, Yohei
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2020, 55 (02) : 179 - 196
[4] Tetrahymena IFT122A is not essential for cilia assembly but plays a role in returning IFT proteins from the ciliary tip to the cell body
Tsao, Che-Chia
Gorovsky, Martin A.
JOURNAL OF CELL SCIENCE, 2008, 121 (04) : 428 - 436
[5] Assembly of IFT Trains at the Ciliary Base Depends on IFT74
Brown, Jason M.
Cochran, Deborah A.
Craige, Branch
Kubo, Tomohiro
Witman, George B.
CURRENT BIOLOGY, 2015, 25 (12) : 1583 - 1593
[6] IFT88 and Ciliary IFT B Complex Members in Mitosis.
Bright, A.
Doxsey, S.
MOLECULAR BIOLOGY OF THE CELL, 2011, 22
[7] IFT27 Links the BBSome to IFT for Maintenance of the Ciliary Signaling Compartment
Eguether, Thibaut
San Agustin, Jovenal T.
Keady, Brian T.
Jonassen, Julie A.
Liang, Yinwen
Francis, Richard
Tobita, Kimimasa
Johnson, Colin A.
Abdelhamed, Zakia A.
Lo, Cecilia W.
Pazour, Gregory J.
DEVELOPMENTAL CELL, 2014, 31 (03) : 279 - 290
[8] IFT25 and IFT27 are required for maintenance of the ciliary signaling
Eguether, T.
Agustin, J. T. San
Keady, B. T.
Jonassen, J. A.
Francis, R.
Liang, Y.
Tobita, K.
Abdel-Hamed, Z.
Johnson, C. A.
Pan, J.
Lo, C. W.
Pazour, G.
MOLECULAR BIOLOGY OF THE CELL, 2013, 24
[9] IFT25 and IFT27 couple the BBSome to the IFT particle for maintenance of the ciliary signaling compartment
Eguether, Thibaut
Pazour, Gregory
FASEB JOURNAL, 2015, 29
[10] Differential expression of IFT molecules in ciliary and non-ciliary cells of the retina
Sedmak, T.
Wolfrum, U.
EUROPEAN JOURNAL OF CELL BIOLOGY, 2010, 89 : 31 - 31

← 1 2 3 4 5 →