Ask about this productRelated genes to: CDC42EP5 antibody
- Gene:
- CDC42EP5 NIH gene
- Name:
- CDC42 effector protein 5
- Previous symbol:
- -
- Synonyms:
- CEP5, Borg3
- Chromosome:
- 19q13.42
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-02
- Date modifiied:
- 2016-01-07
Related products to: CDC42EP5 antibody
Related articles to: CDC42EP5 antibody
- Septin GTPases form hexa- or octameric rods that polymerize into higher order structures and integrate into the cytoskeleton, playing crucial roles in cellular functions. Among these, they are involved in the formation of primary cilia-cellular signaling hubs. It is established that septins localize to cilia and contribute to their formation and function; here, we aim to gain further insights into their oligomeric composition, assembly, and regulation in the confined ciliary compartment. Using cultured cells we demonstrate, that septins enter cilia as octamers and require polymerization for ciliary enrichment. Ciliary localization of septin filaments depends on Borg3, also known as Cdc42ep5, which we identify as an essential component of primary cilia. Knockout of Borg3 as well as dysregulation of Cdc42 impairs septin dynamics and enrichment within cilia. Borg3 localization is regulated by the cycling of the Rho-GTPase Cdc42 between its inactive- and active states confined at the ciliary base. - Source: PubMed
Publication date: 2025/05/12
Schampera Janik NLehmann FriederikeMeléndez Ana ValeriaSchwan Carsten - Single-cell sequencing is an emerging technology that can effectively identify cell types in tumors. In the tumor microenvironment of bladder cancer, macrophages play a crucial role in invasion and immune escape. This study aimed to assess the expression of macrophage-related genes (MRGs) in the tumor microenvironment of bladder cancer patients and construct a prognostic model based on MRGs using bioinformatics methods. - Source: PubMed
Publication date: 2024/06/25
Wang WeizhuoShen JunhengSong DalongFu KaiFu Xu - Identification and validation of genes that functionally account for the growth and metastasis of prostate cancer. - Source: PubMed
Wang WeiYuan DongboJiang KehuaLi RuidongQu HanJiang Fu-NengZhong Wei-DeSun FaJia ZhenyuZhu Jianguo - Cell resistance to taxanes involves several complementary mechanisms, among which septin relocalization from actin stress fibers to microtubules plays an early role. By investigating the molecular mechanism underlying this relocalization, we found that acute paclitaxel treatment triggers the release from stress fibers and subsequent proteasome-mediated degradation of binder of Rho GTPases 2 (BORG2)/Cdc42 effector protein 3 (Cdc42EP3) and to a lesser extent of BORG3/Cdc42EP5, two Cdc42 effectors that link septins to actin in interphase cells. BORG2 or BORG3 silencing not only caused septin detachment from stress fibers but also mimicked the effects of paclitaxel by triggering both septin relocalization to microtubules and significant drug resistance. Conversely, BORG2 or BORG3 overexpression retained septins on actin fibers even after paclitaxel treatment, without affecting paclitaxel sensitivity. We found that drug-induced inhibition of Cdc42 resulted in a drop in BORG2 level and in the relocalization of septins to microtubules. Accordingly, although septins relocalized when overexpressing an inactive mutant of Cdc42, the expression of a constitutively active mutant acted locally at actin stress fibers to prevent septin release, even after paclitaxel treatment. These findings reveal the role of Cdc42 upstream of BORG2 and BORG3 in controlling the interplay between septins, actin fibers, and microtubules in basal condition and in response to taxanes. - Source: PubMed
Publication date: 2021/07/29
Salameh JoëlleCantaloube IsabelleBenoit BéatricePoüs ChristianBaillet Anita - Fast amoeboid migration is critical for developmental processes and can be hijacked by cancer cells to enhance metastatic dissemination. This migratory behavior is tightly controlled by high levels of actomyosin contractility, but how it is coupled to other cytoskeletal components is poorly understood. Septins are increasingly recognized as novel cytoskeletal components, but details on their regulation and contribution to migration are lacking. Here, we show that the septin regulator Cdc42EP5 is consistently required for amoeboid melanoma cells to invade and migrate into collagen-rich matrices and locally invade and disseminate in vivo. Cdc42EP5 associates with actin structures, leading to increased actomyosin contractility and amoeboid migration. Cdc42EP5 affects these functions through SEPT9-dependent F-actin cross-linking, which enables the generation of F-actin bundles required for the sustained stabilization of highly contractile actomyosin structures. This study provides evidence that Cdc42EP5 is a regulator of cancer cell motility that coordinates actin and septin networks and describes a unique role for SEPT9 in melanoma invasion and metastasis. - Source: PubMed
Farrugia Aaron JRodríguez JavierOrgaz Jose LLucas MaríaSanz-Moreno VictoriaCalvo Fernando