A bioactive peptide amidating enzyme is required for ciliogenesis
The pathways controlling cilium biogenesis in different cell types have not been fully elucidated. We recently identified peptidylglycine α-amidating monooxygenase (PAM), an enzyme required for generating amidated bioactive signaling peptides, in Chlamydomonas and mammalian cilia. Here, we show that...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2017-05-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/25728 |
| _version_ | 1811200339042369536 |
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| author | Dhivya Kumar Daniela Strenkert Ramila S Patel-King Michael T Leonard Sabeeha S Merchant Richard E Mains Stephen M King Betty A Eipper |
| author_facet | Dhivya Kumar Daniela Strenkert Ramila S Patel-King Michael T Leonard Sabeeha S Merchant Richard E Mains Stephen M King Betty A Eipper |
| author_sort | Dhivya Kumar |
| collection | DOAJ |
| description | The pathways controlling cilium biogenesis in different cell types have not been fully elucidated. We recently identified peptidylglycine α-amidating monooxygenase (PAM), an enzyme required for generating amidated bioactive signaling peptides, in Chlamydomonas and mammalian cilia. Here, we show that PAM is required for the normal assembly of motile and primary cilia in Chlamydomonas, planaria and mice. Chlamydomonas PAM knockdown lines failed to assemble cilia beyond the transition zone, had abnormal Golgi architecture and altered levels of cilia assembly components. Decreased PAM gene expression reduced motile ciliary density on the ventral surface of planaria and resulted in the appearance of cytosolic axonemes lacking a ciliary membrane. The architecture of primary cilia on neuroepithelial cells in Pam-/- mouse embryos was also aberrant. Our data suggest that PAM activity and alterations in post-Golgi trafficking contribute to the observed ciliogenesis defects and provide an unanticipated, highly conserved link between PAM, amidation and ciliary assembly. |
| first_indexed | 2024-04-12T02:03:13Z |
| format | Article |
| id | doaj.art-2f90b2d4915f465aaa13b927be8c931a |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:03:13Z |
| publishDate | 2017-05-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-2f90b2d4915f465aaa13b927be8c931a2022-12-22T03:52:36ZengeLife Sciences Publications LtdeLife2050-084X2017-05-01610.7554/eLife.25728A bioactive peptide amidating enzyme is required for ciliogenesisDhivya Kumar0https://orcid.org/0000-0002-3737-014XDaniela Strenkert1Ramila S Patel-King2Michael T Leonard3Sabeeha S Merchant4Richard E Mains5https://orcid.org/0000-0003-1154-1331Stephen M King6https://orcid.org/0000-0002-5484-5530Betty A Eipper7https://orcid.org/0000-0003-1171-5557Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, United StatesDepartment of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, United StatesDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, United StatesDepartment of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, United StatesDepartment of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, United States; Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, United StatesDepartment of Neuroscience, University of Connecticut Health Center, Farmington, United StatesDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, United StatesDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, United States; Department of Neuroscience, University of Connecticut Health Center, Farmington, United StatesThe pathways controlling cilium biogenesis in different cell types have not been fully elucidated. We recently identified peptidylglycine α-amidating monooxygenase (PAM), an enzyme required for generating amidated bioactive signaling peptides, in Chlamydomonas and mammalian cilia. Here, we show that PAM is required for the normal assembly of motile and primary cilia in Chlamydomonas, planaria and mice. Chlamydomonas PAM knockdown lines failed to assemble cilia beyond the transition zone, had abnormal Golgi architecture and altered levels of cilia assembly components. Decreased PAM gene expression reduced motile ciliary density on the ventral surface of planaria and resulted in the appearance of cytosolic axonemes lacking a ciliary membrane. The architecture of primary cilia on neuroepithelial cells in Pam-/- mouse embryos was also aberrant. Our data suggest that PAM activity and alterations in post-Golgi trafficking contribute to the observed ciliogenesis defects and provide an unanticipated, highly conserved link between PAM, amidation and ciliary assembly.https://elifesciences.org/articles/25728ciliachlamdyomonasplanariaamidationgolgipeptidylglycine alpha-amidating monooxygenase |
| spellingShingle | Dhivya Kumar Daniela Strenkert Ramila S Patel-King Michael T Leonard Sabeeha S Merchant Richard E Mains Stephen M King Betty A Eipper A bioactive peptide amidating enzyme is required for ciliogenesis eLife cilia chlamdyomonas planaria amidation golgi peptidylglycine alpha-amidating monooxygenase |
| title | A bioactive peptide amidating enzyme is required for ciliogenesis |
| title_full | A bioactive peptide amidating enzyme is required for ciliogenesis |
| title_fullStr | A bioactive peptide amidating enzyme is required for ciliogenesis |
| title_full_unstemmed | A bioactive peptide amidating enzyme is required for ciliogenesis |
| title_short | A bioactive peptide amidating enzyme is required for ciliogenesis |
| title_sort | bioactive peptide amidating enzyme is required for ciliogenesis |
| topic | cilia chlamdyomonas planaria amidation golgi peptidylglycine alpha-amidating monooxygenase |
| url | https://elifesciences.org/articles/25728 |
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