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Poc1B and Sas-6 Function Together during the Atypical Centriole Formation in Drosophila melanogaster.
Jo, Kyoung H; Jaiswal, Ankit; Khanal, Sushil; Fishman, Emily L; Curry, Alaina N; Avidor-Reiss, Tomer.
Affiliation
  • Jo KH; Department of Biological Sciences, University of Toledo, Toledo, OH 43607, USA.
  • Jaiswal A; Department of Biological Sciences, University of Toledo, Toledo, OH 43607, USA.
  • Khanal S; Department of Biological Sciences, University of Toledo, Toledo, OH 43607, USA.
  • Fishman EL; Department of Biological Sciences, University of Toledo, Toledo, OH 43607, USA.
  • Curry AN; Department of Biological Sciences, University of Toledo, Toledo, OH 43607, USA.
  • Avidor-Reiss T; Department of Biological Sciences, University of Toledo, Toledo, OH 43607, USA. tomer.avidorreiss@utoledo.edu.
Cells ; 8(8)2019 08 05.
Article in En | MEDLINE | ID: mdl-31387336
ABSTRACT
Insects and mammals have atypical centrioles in their sperm. However, it is unclear how these atypical centrioles form. Drosophila melanogaster sperm has one typical centriole called the giant centriole (GC) and one atypical centriole called the proximal centriole-like structure (PCL). During early sperm development, centriole duplication factors such as Ana2 and Sas-6 are recruited to the GC base to initiate PCL formation. The centriolar protein, Poc1B, is also recruited at this initiation stage, but its precise role during PCL formation is unclear. Here, we show that Poc1B recruitment was dependent on Sas-6, that Poc1B had effects on cellular and PCL Sas-6, and that Poc1B and Sas-6 were colocalized in the PCL/centriole core. These findings suggest that Sas-6 and Poc1B interact during PCL formation. Co-overexpression of Ana2 and Sas-6 induced the formation of ectopic particles that contained endogenous Poc1 proteins and were composed of PCL-like structures. These structures were disrupted in Poc1 mutant flies, suggesting that Poc1 proteins stabilize the PCL-like structures. Lastly, Poc1B and Sas-6 co-overexpression also induced the formation of PCL-like structures, suggesting that they can function together during the formation of the PCL. Overall, our findings suggest that Poc1B and Sas-6 function together during PCL formation.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Centrioles / Cytoskeletal Proteins / Drosophila Proteins Limits: Animals Language: En Journal: Cells Year: 2019 Document type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Centrioles / Cytoskeletal Proteins / Drosophila Proteins Limits: Animals Language: En Journal: Cells Year: 2019 Document type: Article Affiliation country: United States