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PXD033717

PXD033717 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleTbPH1/TbKifX2 depletion proteome
DescriptionKinesins are motor proteins found in all eukaryotic lineages that move along microtubules to mediate Kinesins are motor proteins found in all eukaryotic lineages that move along microtubules to mediate cellular processes such as mitosis and intracellular transport. In trypanosomatids, the kinesin superfamily has undergone a prominent expansion, resulting in one of the most diverse kinesin repertoires that includes the two kinetoplastid-restricted families X1 and X2. Here, we characterize in Trypanosoma brucei TbKifX2A, an orphaned X2 kinesin. TbKifX2A tightly interacts with TbPH1, a kinesin-like protein with a likely inactive motor domain, a rarely reported occurrence. Both TbKifX2A and TbPH1 localize to the microtubule quartet (MtQ), a characteristic but poorly understood cytoskeletal structure that wraps around the flagellar pocket as it extends to the cell body anterior. The proximal proteome of TbPH1 revealed two other interacting proteins, the flagellar pocket protein FP45 and intriguingly another X2 kinesin, TbKifX2C. Simultaneous ablation of TbKifX2A/TbPH1 results in the depletion of FP45 and TbKifX2C and also an expansion of the flagellar pocket, among other morphological defects. TbKifX2A is the first motor protein to be localized to the MtQ. The observation that TbKifX2C also associates with the MtQ suggests that the X2 kinesin family may have co-evolved with the MtQ, both kinetoplastid-specific traits.cellular processes such as mitosis and intracellular transport. In trypanosomatids, the kinesin superfamily has undergone a prominent expansion, resulting in one of the most diverse kinesin repertoires that includes the two kinetoplastid-restricted families X1 and X2. Here, we characterize in Trypanosoma brucei TbKifX2A, an orphaned X2 kinesin. TbKifX2A tightly interacts with TbPH1, a kinesin-like protein with a likely inactive motor domain, a rarely reported occurrence. Both TbKifX2A and TbPH1 localize to the microtubule quartet (MtQ), a characteristic but poorly understood cytoskeletal structure that wraps around the flagellar pocket as it extends to the cell body anterior. The proximal proteome of TbPH1 revealed two other interacting proteins, the flagellar pocket protein FP45 and intriguingly another X2 kinesin, TbKifX2C. Simultaneous ablation of TbKifX2A/TbPH1 results in the depletion of FP45 and TbKifX2C and also an expansion of the flagellar pocket, among other morphological defects. TbKifX2A is the first motor protein to be localized to the MtQ. The observation that TbKifX2C also associates with the MtQ suggests that the X2 kinesin family may have co-evolved with the MtQ, both kinetoplastid-specific traits.
HostingRepositoryPRIDE
AnnounceDate2022-06-30
AnnouncementXMLSubmission_2022-06-30_01:31:21.516.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterCorinna Benz
SpeciesList scientific name: Trypanosoma brucei; NCBI TaxID: 5691;
ModificationListmethylthiolated residue; acetylated residue; monohydroxylated residue
InstrumentOrbitrap Exploris 480
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-05-05 01:29:09ID requested
12022-06-30 01:31:22announced
Publication List
Benz C, M, ü, ller N, Kaltenbrunner S, V, á, chov, á H, Vancov, á M, Luke, š J, Varga V, Hashimi H, Kinetoplastid-specific X2-family kinesins interact with a kinesin-like pleckstrin homology domain protein that localizes to the trypanosomal microtubule quartet. Mol Microbiol, 118(3):155-174(2022) [pubmed]
Keyword List
submitter keyword: Trypanosoma brucei, kinesin, RNAi
Contact List
Julius Lukes
contact affiliationInstitute of Parasitology, Biology Center, Czech Academy of Sciences, Branišovská 31, 370 05 České Budějovice, CZECH REPUBLIC
contact emailjula@paru.cas.cz
lab head
Corinna Benz
contact affiliationInstitute of Parasitology Biology Center, Czech Academy of Sciences Branišovská 31 370 05 České Budějovice
contact emailcorinna.benz@paru.cas.cz
dataset submitter
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