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The centriole and basal body (CBB) structure nucleates cilia and flagella, and is an essential component of the centrosome, underlying eukaryotic microtubule-based motility, cell division and polarity. In recent years, components of the CBB-assembly machinery have been identified, but little is known about their regulation and evolution. Given the diversity of cellular contexts encountered in eukaryotes, but the remarkable conservation of CBB morphology, we asked whether general mechanistic principles could explain CBB assembly. We analysed the distribution of each component of the human CBB-assembly machinery across eukaryotes as a strategy to generate testable hypotheses. We found an evolutionarily cohesive and ancestral module, which we term UNIMOD and is defined by three components (SAS6, SAS4/CPAP and BLD10/CEP135), that correlates with the occurrence of CBBs. Unexpectedly, other players (SAK/PLK4, SPD2/CEP192 and CP110) emerged in a taxon-specific manner. We report that gene duplication plays an important role in the evolution of CBB components and show that, in the case of BLD10/CEP135, this is a source of tissue specificity in CBB and flagella biogenesis. Moreover, we observe extreme protein divergence amongst CBB components and show experimentally that there is loss of cross-species complementation among SAK/PLK4 family members, suggesting species-specific adaptations in CBB assembly. We propose that the UNIMOD theory explains the conservation of CBB architecture and that taxon- and tissue-specific molecular innovations, gained through emergence, duplication and divergence, play important roles in coordinating CBB biogenesis and function in different cellular contexts.

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Autor(es)

Carvalho -  Santos, Z. -  Machado, P. -  Branco, P. -  Tavares -  Cadete, F. -  Rodrigues -  Martins, A. -  Pereira -  Leal, J. B. -  Bettencourt -  Dias, M. - 

Id.: 69363971

Idioma: eng  - 

Versión: 1.0

Estado: Final

Palabras claveCentriole - 

Tipo de recurso: article  - 

Tipo de Interactividad: Expositivo

Nivel de Interactividad: muy bajo

Audiencia: Estudiante  -  Profesor  -  Autor  - 

Estructura: Atomic

Coste: no

Copyright: sí

: openAccess

Requerimientos técnicos:  Browser: Any - 

Relación: [References] info:eu-repo/grantAgreement/FCT/3599-PPCDT/73195/PT
[References] info:eu-repo/grantAgreement/FCT/3599-PPCDT/73194/PT
[References] http://jcs.biologists.org/content/123/9/1414

Fecha de contribución: 04-dic-2016

Contacto:

Localización:
* Stepwise evolution of the centriole-assembly pathway Zita Carvalho-Santos, Pedro Machado, Pedro Branco, Filipe Tavares-Cadete, Ana Rodrigues-Martins, José B. Pereira-Leal, Mónica Bettencourt-Dias J Cell Sci 2010 123: 1414-1426; doi: 10.1242/jcs.064931
* 10.1242/jcs.064931

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Otros recursos de la mismacolección

  1. Evolution: Tracing the origins of centrioles, cilia, and flagella This deposit is composed by the main article plus the supplementary materials of the publication.
  2. Centrosomes and cilia in human disease The deposited article is a post-print version (NIH-PA Author Manuscript) and has been submitted to p...
  3. BLD10/CEP135 Is a Microtubule-Associated Protein that Controls the Formation of the Flagellum Central Microtubule Pair The deposited article is a post-print version and has been submitted to peer review.
  4. A structural road map to unveil basal body composition and assembly The deposited article is a post-print version and has been submitted to peer review.
  5. Regulation of Autophosphorylation Controls PLK4 Self-Destruction and Centriole Number The deposited article is a post-print version and has been submitted to peer review.

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