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PRC1 phosphorylation by CDK1 and PLK1

ABSTRACT: This work study the effects of PRC1 phosphorylation by CDK1 and PLK1.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Wei Ming Lim

LAB HEAD: Thomas Surrey

PROVIDER: PXD055933 | Pride | 2024-11-01

REPOSITORIES: Pride

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			Action	DRS
	2020MA007_WELI_001_01_mixV2_30pto.msf	Msf
	2020MA007_WELI_001_01_mixV2_30pto.raw	Raw
	2020MA007_WELI_002_01_mixV2_30pto.msf	Msf
	2020MA007_WELI_002_01_mixV2_30pto.raw	Raw
	2020MA007_WELI_003_01_mixV2_30pto.msf	Msf

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Publications

Regulation of minimal spindle midzone organization by mitotic kinases.

Lim Wei Ming WM Chew Wei-Xiang WX Esposito Verza Arianna A Pesenti Marion M Musacchio Andrea A Surrey Thomas T

Nature communications 20241029 1

During cell division, the microtubule cytoskeleton undergoes dramatic cell cycle-driven reorganizations of its architecture. Coordinated by changes in the phosphorylation patterns of a multitude of microtubule associated proteins, the mitotic spindle first self-assembles to capture the chromosomes and then reorganizes in anaphase as the chromosomes are segregated. A key protein for this reorganization is PRC1 which is differentially phosphorylated by the mitotic kinases CDK1 and PLK1. How the ph ...[more]

PMID: 39472429

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AMBRA1 phosphorylation by CDK1 and PLK1 regulates mitotic spindle orientation.

Project description:AMBRA1 is a crucial factor for nervous system development, and its function has been mainly associated with autophagy. It has been also linked to cell proliferation control, through its ability to regulate c-Myc and D-type cyclins protein levels, thus regulating G1-S transition. However, it remains still unknown whether AMBRA1 is differentially regulated during the cell cycle, and if this pro-autophagy protein exerts a direct role in controlling mitosis too. Here we show that AMBRA1 is phosphorylated during mitosis on multiple sites by CDK1 and PLK1, two mitotic kinases. Moreover, we demonstrate that AMBRA1 phosphorylation at mitosis is required for a proper spindle function and orientation, driven by NUMA1 protein. Indeed, we show that the localization and/or dynamics of NUMA1 are strictly dependent on AMBRA1 presence, phosphorylation and binding ability. Since spindle orientation is critical for tissue morphogenesis and differentiation, our findings could account for an additional role of AMBRA1 in development and cancer ontogenesis.

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Differential control of Eg5-dependent centrosome separation by Plk1 and Cdk1.

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The role of Cdk1-cyclin B in G1/S transition revealed by chemical genetic inhibition of Cdc7

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