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PXD074602-1
PXD074602 is an original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Identification of a component of the Tubulin Poly-glutamylase Complex required for phosphoinositide homeostasis and cilium assembly and maintenance |
| Description | The tubulin poly-glutamylase complex (TPGC) is comprised of TTLL1 and at least five associated proteins that promote the addition of glutamate residues to carboxy-terminal tails of tubulin subunits comprising microtubules. Despite its discovery two decades ago, the enzyme has been refractory to characterization owing to its complex multimeric nature and the inability to detect poly-glutamylase activity after assembling the six-subunit complex. We now show that TPGC is the key enzyme driving centriolar and ciliary poly-glutamylation. We identified two additional TPGC subunits, TBC1D19 and KIAA1841, and showed that both components play an essential role in the assembly of the eight-subunit holo-enzyme. We were able to reconstitute the activity of TPGC with all eight subunits. TBC1D19 and KIAA1841 were essential for TPGC activity, and loss of TBC1D19 strongly compromised multiple tubulin modifications, including axonemal poly-glutamylation. TBC1D19 loss also abolished transport of Arl13b and other ciliary membrane proteins, abrogating primary cilium assembly. Structural predictions suggested an essential role for TBC1D19 and KIAA1841 in complex assembly, microtubule binding, and preferential poly-glutamylation of alpha-tubulin. We found that TBC1D19 loss abrogated the ciliary localization of phosphatidyl inositol phosphatase, INPP5E, which coincided with cilium instability. Ciliogenesis in TBC1D19 null cells could be restored through inhibition of a specific phosphatidyl inositol phosphate (PIP) kinase, PIP5K1c, suggesting that TBC1D19 is required to maintain PIP homeostasis during ciliogenesis. Collectively, our data show that TPGC is a multi-functional enzyme essential for cilium assembly and maintenance. This entry contains the raw mass spectrometric data, methods and results for the affinity purification of TBC1D19. |
| HostingRepository | MassIVE |
| AnnounceDate | 2026-02-18 |
| AnnouncementXML | Submission_2026-02-18_12:22:06.820.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Non peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Beatrix Ueberheide |
| SpeciesList | scientific name: Homo sapiens; common name: human; NCBI TaxID: 9606; |
| ModificationList | Oxidation; Deamidated |
| Instrument | Q Exactive HF-X |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|---|---|---|
| 0 | 2026-02-18 11:58:04 | ID requested | |
| ⏵ 1 | 2026-02-18 12:22:07 | announced |
Publication List
| no publication |
Keyword List
| submitter keyword: tubulin poly-glutamylase complex, poly-glutamylation, DatasetType:Proteomics |
Contact List
| Beatrix M Ueberheide | |
|---|---|
| contact affiliation | NYU Langone Grossman School of Medicine |
| contact email | beatrix.ueberheide@nyulangone.org |
| lab head | |
| Beatrix Ueberheide | |
| contact affiliation | NYU School of Medicine |
| contact email | beatrixueberheide@gmail.com |
| dataset submitter | |
Full Dataset Link List
| MassIVE dataset URI |
| 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://massive-ftp.ucsd.edu/v12/MSV000100885/ |
