PXD074179-1

PXD074179 is an original dataset announced via ProteomeXchange.

Title	CDK1-dependent N-terminal NuMA phosphorylation promotes dynein-dynactin-NuMA assembly for accurate chromosome segregation
Description	The microtubule-based motor dynein and its cofactor dynactin are activated by various adaptors to fulfil essential functions throughout the cell cycle, including organelle transport and mitotic spindle assembly. NuMA is a mitotic adaptor that interacts with dynein-dynactin via its N-terminal region (NuMA-N). However, how NuMA-N binds and activates dynein-dynactin in mitosis remains unclear. Here, we combine a membrane-tethering assay, quantitative proteomics, and live-cell analyses to show that mitotic phosphorylation of NuMA-N drives dynein-dynactin-NuMA (DDN) assembly. We find that CDK1-Cyclin B1 phosphorylates NuMA-N, primarily at its conserved serine 203, which stimulates dynein activation in vitro. Replacing endogenous NuMA with phosphorylation-deficient mutants further reveals that NuMA-N phosphorylation, together with its dynein-binding site and Spindly-like motif, is required to form stable DDN complexes for functional spindle assembly. These results highlight CDK1-dependent N-terminal NuMA phosphorylation as a crucial mitotic phospho-switch that ensures stable multivalent interactions between dynein-dynactin and NuMA for accurate chromosome segregation.
HostingRepository	PRIDE
AnnounceDate	2026-02-10
AnnouncementXML	Submission_2026-02-09_19:07:50.093.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Marvin van Toorn
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationList	phosphorylated residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2026-02-07 05:50:48	ID requested
⏵ 1	2026-02-09 19:07:50	announced

Dataset with its publication pending

submitter keyword: None

Tomomi Kiyomitsu
contact affiliation	Okinawa Institute of Science and Technology (OIST), Okinawa, Japan
contact email	tomomi.kiyomitsu@oist.jp
lab head
Marvin van Toorn
contact affiliation	Okinawa Institute of Science and Technology (OIST), Okinawa, Japan
contact email	marvinvtoorn@pm.me
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD074179
     1. Label: PRIDE project
     2. Name: CDK1-dependent N-terminal NuMA phosphorylation promotes dynein-dynactin-NuMA assembly for accurate chromosome segregation