{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hwang J"],"funding":["University of Minnesota","Children's Discovery Institute","National Institutes of Health","Children's Discovery Institute","NIGMS NIH HHS","NIH HHS","National Science Foundation"],"pagination":["539-555"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12239100"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["81(11)"],"pubmed_abstract":["To identify proteins specific to the proximal ciliary axoneme, we used iTRAQ to compare short (~2 μm) and full-length (~11 μm) axonemes of Chlamydomonas. Known components of the proximal axoneme such as minor dynein heavy chains and LF5 kinase as well as the ciliary tip proteins FAP256 (CEP104) and EB1 were enriched in short axonemes whereas proteins present along the length of the axoneme were of similar abundance in both samples. The iTRAQ analysis revealed that FAP93, a protein of unknown function, and protein phosphatase 2A (PP2A) are enriched in the short axonemes. Consistently, immunoblots show enrichment of FAP93 and PP2A in short axonemes and immunofluorescence confirms the localization of FAP93 and enrichment of PP2A at the proximal axoneme. Ciliary regeneration reveals that FAP93 assembles continuously but more slowly than other axonemal structures and terminates at 1.03 μm in steady-state axonemes. The length of FAP93 assembly correlates with ciliary length, demonstrating ciliary length-dependent assembly of FAP93. Dikaryon rescue experiments show that FAP93 can assemble independently of IFT transport. In addition, FRAP analysis of GFP-tagged FAP93 demonstrates that FAP93 is stably anchored in the axoneme. FAP93 may function as a scaffold for assembly of other specific proteins at the proximal axoneme."],"journal":["Cytoskeleton (Hoboken, N.J.)"],"pubmed_title":["Assembly of FAP93 at the proximal axoneme in Chlamydomonas cilia."],"pmcid":["PMC12239100"],"funding_grant_id":["R01 GM051173","R01 GM110413","R37 GM051173","R35 GM131909","R37 GM055667","R01 GM055667"],"pubmed_authors":["Fox LA","Stuart CDE","Alford LM","Gordon SA","Yanagisawa H","Bower R","Porter ME","Hunter EL","Hwang J","Davis KC","Goodwin RE","Dutcher SK","Jimenez AR","Lechtreck KF","Sale WS"],"additional_accession":[]},"is_claimable":false,"name":"Assembly of FAP93 at the proximal axoneme in Chlamydomonas cilia.","description":"To identify proteins specific to the proximal ciliary axoneme, we used iTRAQ to compare short (~2 μm) and full-length (~11 μm) axonemes of Chlamydomonas. Known components of the proximal axoneme such as minor dynein heavy chains and LF5 kinase as well as the ciliary tip proteins FAP256 (CEP104) and EB1 were enriched in short axonemes whereas proteins present along the length of the axoneme were of similar abundance in both samples. The iTRAQ analysis revealed that FAP93, a protein of unknown function, and protein phosphatase 2A (PP2A) are enriched in the short axonemes. Consistently, immunoblots show enrichment of FAP93 and PP2A in short axonemes and immunofluorescence confirms the localization of FAP93 and enrichment of PP2A at the proximal axoneme. Ciliary regeneration reveals that FAP93 assembles continuously but more slowly than other axonemal structures and terminates at 1.03 μm in steady-state axonemes. The length of FAP93 assembly correlates with ciliary length, demonstrating ciliary length-dependent assembly of FAP93. Dikaryon rescue experiments show that FAP93 can assemble independently of IFT transport. In addition, FRAP analysis of GFP-tagged FAP93 demonstrates that FAP93 is stably anchored in the axoneme. FAP93 may function as a scaffold for assembly of other specific proteins at the proximal axoneme.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-06-05T08:49:17.829Z","creation":"2026-05-14T03:12:17.95Z"},"accession":"S-EPMC12239100","cross_references":{"pubmed":["38224153"],"doi":["10.1002/cm.21818"]}}