EMD-4927
Junction between microtubule triplet of isolated Paramecium tetraurelia centriole - inner core region
EMD-4927
Subtomogram averaging32.7 Å
Deposition: 02/05/2019Map released: 26/02/2020
Last modified: 11/03/2020
Sample Organism:
Paramecium tetraurelia
Sample: Junction between microtubule triplet of isolated Paramecium tetraurelia centriole - inner core region
Deposition Authors: Le Guennec M, Klena N, Tassin AM, Van der Hoek H, Erdmann PS, Schaffer M, Kovacik L, Goldie KN, Stahlberg H, Engel BD, Hamel V, Guichard P
Sample: Junction between microtubule triplet of isolated Paramecium tetraurelia centriole - inner core region
Deposition Authors: Le Guennec M, Klena N, Tassin AM, Van der Hoek H, Erdmann PS, Schaffer M, Kovacik L, Goldie KN, Stahlberg H, Engel BD, Hamel V, Guichard P
A helical inner scaffold provides a structural basis for centriole cohesion.
Le Guennec M 
,
Klena N ,
Gambarotto D ,
Laporte MH ,
Tassin AM,
van den Hoek H ,
Erdmann PS,
Schaffer M,
Kovacik L ,
Borgers S,
Goldie KN,
Stahlberg H ,
Bornens M ,
Azimzadeh J ,
Engel BD ,
Hamel V ,
Guichard P
(2020) Sci Adv , 6 , eaaz4137 - eaaz4137
,
Klena N ,
Gambarotto D ,
Laporte MH ,
Tassin AM,
van den Hoek H ,
Erdmann PS,
Schaffer M,
Kovacik L ,
Borgers S,
Goldie KN,
Stahlberg H ,
Bornens M ,
Azimzadeh J ,
Engel BD ,
Hamel V ,
Guichard P
(2020) Sci Adv , 6 , eaaz4137 - eaaz4137
Abstract:
The ninefold radial arrangement of microtubule triplets (MTTs) is the hallmark of the centriole, a conserved organelle crucial for the formation of centrosomes and cilia. Although strong cohesion between MTTs is critical to resist forces applied by ciliary beating and the mitotic spindle, how the centriole maintains its structural integrity is not known. Using cryo-electron tomography and subtomogram averaging of centrioles from four evolutionarily distant species, we found that MTTs are bound together by a helical inner scaffold covering ~70% of the centriole length that maintains MTTs cohesion under compressive forces. Ultrastructure Expansion Microscopy (U-ExM) indicated that POC5, POC1B, FAM161A, and Centrin-2 localize to the scaffold structure along the inner wall of the centriole MTTs. Moreover, we established that these four proteins interact with each other to form a complex that binds microtubules. Together, our results provide a structural and molecular basis for centriole cohesion and geometry.
The ninefold radial arrangement of microtubule triplets (MTTs) is the hallmark of the centriole, a conserved organelle crucial for the formation of centrosomes and cilia. Although strong cohesion between MTTs is critical to resist forces applied by ciliary beating and the mitotic spindle, how the centriole maintains its structural integrity is not known. Using cryo-electron tomography and subtomogram averaging of centrioles from four evolutionarily distant species, we found that MTTs are bound together by a helical inner scaffold covering ~70% of the centriole length that maintains MTTs cohesion under compressive forces. Ultrastructure Expansion Microscopy (U-ExM) indicated that POC5, POC1B, FAM161A, and Centrin-2 localize to the scaffold structure along the inner wall of the centriole MTTs. Moreover, we established that these four proteins interact with each other to form a complex that binds microtubules. Together, our results provide a structural and molecular basis for centriole cohesion and geometry.