PXD058873

PXD058873 is an original dataset announced via ProteomeXchange.

Title	Phylo-proteomics Reveals Conserved Patterns of Axonemal Dynein Methylation Across the Motile Ciliated Eukaryotes (addendum)
Description	Assembly of the axonemal dynein motors that power ciliary motility occurs in the cytoplasm. Studies in a broad array of organisms have revealed that at least nineteen cytosolic factors are specifically required for this process. Recently, one of these factors (DNAAF3/PF22) was identified as an S-adenosylmethionine-dependent methyltransferase. Furthermore, examination of dyneins from the green alga Chlamydomonas found that axonemal dyneins are methylated at sub-stoichiometric levels on multiple sites including key Lys and Arg residues in several of the nucleotide binding domains and on the microtubule-binding region. Given the highly conserved nature of axonemal dyneins and their cytoplasmic assembly factors, one key question is whether methylation is exclusively present only in dyneins from the chlorophyte algae, or if these modifications occur more broadly throughout the motile ciliated eukaryotes. Here we take a phylo-proteomic approach and examine dynein methylation in a wide range of eukaryotic organisms bearing motile cilia. We find unambiguous evidence for methylation of axonemal dyneins in alveolates, chlorophytes, trypanosomes, and throughout most of the metazoa, including ctenophores, echinoderms, mollusks, ascidians, and vertebrates. Intriguingly, we were unable to identify a single instance of methylation on Drosophila sperm dynein even though dipterans express a Dnaaf3 ortholog, or in spermatozoids of the fern Ceratopteris which assembles inner arms but lacks both outer arm dyneins and DNAAF3. Thus, methylation is a post-translational feature of axonemal dyneins that has been broadly conserved in most eukaryotic groups suggesting the existence of a post-translational dynein code that variably modifies the function of these motors.
HostingRepository	PRIDE
AnnounceDate	2025-02-20
AnnouncementXML	Submission_2025-02-20_07:21:16.168.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jeremy Balsbaugh
SpeciesList	scientific name: Chlamydomonas sp. HS-5; NCBI TaxID: 108458; scientific name: Drosophila willistoni; NCBI TaxID: 7260;
ModificationList	monomethylated residue; trimethylated residue; phosphorylated residue; acetylated residue; monohydroxylated residue; dimethylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Eclipse

Revision	Datetime	Status	ChangeLog Entry
0	2024-12-14 12:54:37	ID requested
⏵ 1	2025-02-20 07:21:16	announced

Sakato-Antoku M, Patel N, Inaba M, Rao Q, Yang J, Patel-King RS, Inaba K, Balsbaugh JL, King SM, Phyloproteomics reveals conserved patterns of axonemal dynein methylation across the motile ciliated eukaryotes. Mol Biol Cell, 36(4):ar49(2025) [pubmed]

10.1091/mbc.e25-02-0055;

submitter keyword: DHC, methylation, dynein, phosphorylation,cilia, drosophila

Jeremy Balsbaugh
contact affiliation	Proteomics & Metabolomics Facility, Center for Open Research Resources & Equipment University of Connecticut Storrs, CT 06269
contact email	jeremy.balsbaugh@uconn.edu
lab head
Jeremy Balsbaugh
contact affiliation	University of Connecticut
contact email	jeremy.balsbaugh@uconn.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/02/PXD058873

PRIDE project URI

• PRIDE
  1. PXD058873
     1. Label: PRIDE project
     2. Name: Phylo-proteomics Reveals Conserved Patterns of Axonemal Dynein Methylation Across the Motile Ciliated Eukaryotes (addendum)