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Last update 08 May 2025

CEP192

Last update 08 May 2025

Basic Info

Synonyms

centrosomal protein 192, Centrosomal protein of 192 kDa, CEP192

+ [4]

Introduction

Required for mitotic centrosome maturation and bipolar spindle assembly (PubMed:17980596, PubMed:18207742, PubMed:25042804). Appears to be a major regulator of pericentriolar material (PCM) recruitment, centrosome maturation, and centriole duplication (PubMed:17980596, PubMed:18207742, PubMed:25042804). Centrosome-specific activating scaffold for AURKA and PLK1 (PubMed:25042804).

Drugs associated with CEP192

CB-039

Target

CEP192

Mechanism

CEP192 inhibitors

Active Org.

Shanghai Institute of Materia Medica Chinese Academy of Sci

Originator Org.

Shanghai Institute of Materia Medica Chinese Academy of Sci

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with CEP192

100 Translational Medicine associated with CEP192

0 Patents (Medical) associated with CEP192

Literatures (Medical) associated with CEP192

01 Jul 2025·Journal of Molecular Biology

PLK4 Homodimerization is Required for CEP152 Centrosome Localization and Spindle Organization

Article

Author: Singh, Priyanka ; Sanghi, Srishti ; Kasera, Harshita

The centrosome-specific Polo-Like Kinase 4 (PLK4) is a unique serine/threonine kinase family member that homodimerizes using its cryptic polo-box (CPB) region. PLK4 homodimerization causes transphosphorylation, which activates its ubiquitin-mediated degradation. The same CPB interacts with upstream centrosome recruiters, CEP152 and CEP192 in human cells. However, the involvement of PLK4 homodimerization with the CEP192-CEP152 network remains unexplored. This work identified a cancerous PLK4 variant, which truncated the protein to disrupt the CPB at 774 residue. The truncated PLK4 is unable to homodimerize or interact with CEP152 or CEP192. During the S-phase, CEP152 recruits PLK4 to centrosomes, and the homodimerization of PLK4 is needed to maintain CEP152 at centrosomes. The reduction in levels of CEP152 on PLK4 homodimerization mutant expression correlates to pericentrin at S-phase centrosomes, which causes unfocussed spindles at the M-phase and reduces cell viability. The work shows a cross-dependency between CEP152 and PLK4 homodimerization for centrosome functioning, which is disrupted in cancer.

10 Apr 2025·Journal of Medicinal Chemistry

Synthesis of an RBM39 Degrader That Downregulates CEP192 and Induces Disorganized Spindle Structures

Article

Author: Huang, He ; Zhang, Shijie ; Lu, Yuhan ; Zhao, Yujun ; Cheng, Ying ; Ren, Xuelian ; Chen, Yi ; Lyu, Xilin ; Yan, Ziqin ; Wang, Zhiyi ; Cheng, Jing ; Wang, Chenxu ; Wang, Xiancheng ; Lin, Dongze ; Su, Yi

RBM39 is an essential component of the spliceosome, playing a critical role in maintaining mRNA integrity. Its depletion significantly exacerbates RNA splicing defects and demonstrates potent anticancer activity. To identify key effectors following RBM39 depletion, we employed a multiomics approach to directly compare two structurally distinct compounds, CB039 and Indisulam. Through proteomic analysis, RNA sequencing, and DepMap dependency assessment, CEP192 emerged as a crucial gene, exhibiting dependency in 96% of the 1,100 analyzed cancer cell lines. In eight cancer cell lines, treatment with both CB039 and Indisulam consistently induced CEP192 exon 42 skipping and reduced CEP192 protein levels. Mechanistically, either CB039 treatment or RNA interference-mediated CEP192 knockdown led to a significant increase in spindle disorganization, as well as chromosome condensation and failed segregation. In conclusion, our characterization of the downstream effects of RBM39 depletion provides novel insights into the therapeutic potential of RBM39 degraders.

21 Mar 2025·Science Advances

The conserved Spd-2/CEP192 domain adopts a unique protein fold to promote centrosome scaffold assembly

Article

Author: Wainman, Alan ; Sheppard, Devon ; Feng, Zhe ; Lea, Susan M. ; Raff, Jordan W. ; Cottee, Matthew ; Alvarez-Rodrigo, Ines ; Andreeva, Antonina ; Saurya, Saroj ; Johnson, Steven ; Hu, Liuyi ; van Breugel, Mark ; Apizi, Muladili ; Wong, Siu-Shing

Centrosomes form when centrioles assemble pericentriolar material (PCM) around themselves. Spd-2/CEP192 proteins, defined by a conserved “Spd-2 domain” (SP2D) comprising two closely spaced AspM-Spd-2-Hydin (ASH) domains, play a critical role in centrosome assembly. Here, we show that the SP2D does not target Drosophila Spd-2 to centrosomes but rather promotes PCM scaffold assembly. Crystal structures of the human and honeybee SP2D reveal an unusual “extended cradle” structure mediated by a conserved interaction interface between the two ASH domains. Mutations predicted to perturb this interface, including a human mutation associated with male infertility and Mosaic Variegated Aneuploidy, disrupt PCM scaffold assembly in flies. The SP2D is monomeric in solution, but the Drosophila SP2D can form higher-order oligomers upon phosphorylation by PLK1 (Polo-like kinase 1). Crystal-packing interactions and AlphaFold predictions suggest how SP2Ds might self-assemble, and mutations associated with one such potential dimerization interface markedly perturb SP2D oligomerization in vitro and PCM scaffold assembly in vivo.

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