Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling.

eLife - 24 Sept 2013

Primorac Ivana, Weir John R, Chiroli Elena, Gross Fridolin, Hoffmann Ingrid, van Gerwen Suzan, Ciliberto Andrea, Musacchio Andrea

Abstract excerpt

Regulation of macromolecular interactions by phosphorylation is crucial in signaling networks. In the spindle assembly checkpoint (SAC), which enables errorless chromosome segregation, phosphorylation promotes recruitment of SAC proteins to tensionless kinetochores. The SAC kinase Mps1 phosphorylates multiple Met-Glu-Leu-Thr (MELT) motifs on the kinetochore subunit Spc105/Knl1. The phosphorylated MELT motifs...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Cycle Proteins
Share to Oligopeptides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphorylation

Share to Poly-ADP-Ribose Binding Proteins

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Share to Signal Transduction

Share to Spindle Apparatus

Source

Open in PubMed Open full text

Identifiers

PMID: 24066227
DOI: 10.7554/eLife.01030
PMCID: PMC3779320

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling.PMID 24066227Read ↗

Sequential multisite phospho-regulation of KNL1-BUB3 interfaces at mitotic kinetochores.Semantic proximity Read ↗

MPS1/Mph1 phosphorylates the kinetochore protein KNL1/Spc7 to recruit SAC components.Semantic proximity Read ↗

Synthetic Physical Interactions Map Kinetochore-Checkpoint Activation Regions.Semantic proximity Read ↗

Mps1 phosphorylates Borealin to control Aurora B activity and chromosome alignment.Semantic proximity Read ↗

Structural and mechanistic insights into Mps1 kinase activation.Semantic proximity Read ↗

Mph1 kinetochore localization is crucial and upstream in the hierarchy of spindle assembly checkpoint protein recruitment to kinetochores.Semantic proximity Read ↗

Microtubule-sliding activity of a kinesin-8 promotes spindle assembly and spindle-length control.Semantic proximity Read ↗

BubR1 recruitment to the kinetochore via Bub1 enhances Spindle Assembly Checkpoint signalingSemantic proximity Read ↗

Dissection of the Spindle Assembly Checkpoint by Proximity ProteomicsSemantic proximity Read ↗

Mps1Mph1 Kinase Phosphorylates Mad3 to Inhibit Cdc20Slp1-APC/C and Maintain Spindle Checkpoint Arrests.Semantic proximity Read ↗

Mps1 phosphorylation of Dam1 couples kinetochores to microtubule plus ends at metaphase.Semantic proximity Read ↗

The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.