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

Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion.

Molecular cell - 7 May 2004

Litvak Vladimir, Argov Rachel, Dahan Nili, Ramachandran Sreekumar, Amarilio Roy, Shainskaya Alla, Lev Sima

Abstract excerpt

The rearrangement of the Golgi apparatus during mitosis is regulated by several protein kinases, including Cdk1 and Plk1. Several peripheral Golgi proteins that dissociate from the Golgi during mitosis are implicated in regulation of cytokinesis or chromosome segregation, thereby coordinating mitotic and cytokinetic events to Golgi rearrangement. Here we show that, at the onset of mitosis, Cdk1 phosphorylates the...

Read the complete abstract on PubMed

Topics

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

Share to Calcium-Binding Proteins
Share to CDC2 Protein Kinase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Eye Proteins

Share to Golgi Apparatus

Share to HeLa Cells

Share to Mitosis

Share to Polo-Like Kinase 1

Share to Protein Kinases

Source

Identifiers

PMID: 15125835
DOI: 10.1016/s1097-2765(04)00214-x

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

Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion.PMID 15125835Read ↗

Physiological Relevance of Cell Cycle KinasesSemantic proximity Read ↗

Phosphorylation of p37 is important for Golgi disassembly at mitosis.Semantic proximity Read ↗

Compartmentalization of the functions and regulation of the mitotic cyclin Clb2 in S. cerevisiae.Semantic proximity Read ↗

Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2.Semantic proximity Read ↗

Temporal control of the dephosphorylation of Cdk substrates by mitotic exit pathways in budding yeast.Semantic proximity Read ↗

Cyclin B1-Cdk1 facilitates MAD1 release from the nuclear pore to ensure a robust spindle checkpoint.Semantic proximity Read ↗

Phosphorylation regulates VCIP135 function in Golgi membrane fusion during the cell cycle.Semantic proximity Read ↗

Dbf2-Mob1 drives relocalization of protein phosphatase Cdc14 to the cytoplasm during exit from mitosis.Semantic proximity Read ↗

Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear envelope breakdown during prophase.Semantic proximity Read ↗

Mitotic phosphorylation of Exo84 disrupts exocyst assembly and arrests cell growth.Semantic proximity Read ↗

CDK1-mediated mitotic phosphorylation of PBK is involved in cytokinesis and inhibits its oncogenic activity.Semantic proximity Read ↗

Sid2p, a spindle pole body kinase that regulates the onset of cytokinesis.Semantic proximity Read ↗

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