DBN1

Last update 08 May 2025

Basic Info

Synonyms

D0S117E, DBN1, Developmentally-regulated brain protein

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Introduction

Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (PubMed:20215400). Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (PubMed:20215400). Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines (By similarity). Involved in memory-related synaptic plasticity in the hippocampus (By similarity).

100 Clinical Results associated with DBN1

100 Translational Medicine associated with DBN1

0 Patents (Medical) associated with DBN1

410

Literatures (Medical) associated with DBN1

01 May 2025·Hepatology

The actin-binding protein drebrin disrupts NF2-LATS kinases complex assembly to facilitate liver tumorigenesis

Article

Author: Zhang, Haijiao ; Xu, Jinjin ; Wei, Henan ; Gao, Haoran ; Zhang, Haoen ; Zhou, Hu ; Lu, Yi ; Wei, Fang ; Yang, Ruizeng ; Sun, Yang ; Li, Xiaoyu ; Zhao, Lihua ; Jin, Yunyun ; Zhang, Lei ; Gao, Daming ; Miao, Sen ; Yu, Wentao ; Li, Jinhui

Background and Aims:The Hippo signaling has emerged as a crucial regulator of tissue homeostasis, regeneration, and tumorigenesis, representing a promising therapeutic target. Neurofibromin 2 (NF2), a component of Hippo signaling, is directly linked to human cancers but has been overlooked as a target for cancer therapy.Approach and Results:Through a high-content RNA interference genome-wide screen, the actin-binding protein Drebrin (DBN1) has been identified as a novel modulator of YAP localization. Further investigations have revealed that DBN1 directly interacts with NF2, disrupting the activation of large tumor suppressor kinases (LATS1/2) by competing with LATS kinases for NF2 binding. Consequently, DBN1 knockout considerably promotes YAP nuclear exclusion and repression of target gene expression, thereby preventing cell proliferation and liver tumorigenesis. We identified three lysine residues (K238, K248, and K252) essential for DBN1-NF2 interaction and developed a mutant DBN1 (DBN1-3Kmut) that is defective in NF2 binding and incompetent to trigger NF2-dependent YAP activation and tumorigenesis both in vitro and in vivo. Furthermore, BTP2, a DBN1 inhibitor, successfully restored NF2-LATS kinase binding and elicited potent antitumor activity. The combination of sorafenib and BTP2 exerted synergistic inhibitory effects against HCC.Conclusions:Our study identifies a novel DBN1-NF2-LATS axis, and pharmacological inhibition of DBN1 represents a promising alternative intervention targeting the Hippo pathway in cancer treatment.

01 May 2025·International Journal of Biological Macromolecules

MAZ-induced lncRNA H19 regulates proliferation and differentiation of porcine skeletal muscle satellite cells via sponge miR-935/miR-296-5p and the p38 MAPK pathway

Article

Author: Fu, Chong ; Liu, Quan ; Li, Mengxun ; Han, Min ; Xie, Su ; Zhou, Honghong ; Li, Changchun

Skeletal muscle satellite cell proliferation and differentiation are important stages in skeletal muscle development, and long non-coding RNAs (lncRNAs) play important roles in both stages. We previously determined the basal functions of lncRNA H19 (H19) and the drebrin 1 (DBN1) gene in porcine skeletal muscle satellite cells (PSCs). However, the mechanisms for H19 and DBN1 regulation of the proliferation and differentiation of PSCs are still unclear. In this study, double luciferase report and pull down results confirmed H19 upregulates DBN1 expression by acting as a miR-935/miR-296-5p decoy. The western blotting results showed upregulated DBN expression activates the p38 mitogen-activated protein kinase (MAPK) pathway to inhibit PSC proliferation and promote differentiation. Moreover, ChIP results showed H19 transcription is regulated by the upstream transcription factor myc-associated zinc finger protein (MAZ). In conclusion, we resolved the mechanism for H19 regulation of proliferation and differentiation of PSCs, contributing to a deeper understanding of the epigenetic regulation of skeletal muscle development and will accelerate advancements in animal genetic improvement.

01 May 2025·Journal of Molecular Biology

Functional Differences Between Neuronal and Non-neuronal Isoforms of Drebrin

Article

Author: Grintsevich, Elena E ; Mkrtchyan, Mikayel ; Srapyan, Sargis ; Berlemont, Renaud

Actin cytoskeleton is vital for neuronal function. Drebrin is a key F-actin binding protein in neurons which is linked to the filaments' stabilization. As mammalian brain develops, drebrin expression pattern switches from non-neuronal (drebrin E, Embryonic) to neuron-specific isoform (drebrin A, Adult), but the evolutionary need for such a switch is enigmatic. Prior in cellulo and in vivo work suggested a non-redundant role of drebrin isoforms in neuronal development and function, however, molecular level understanding of it is lacking. Here we used mutagenesis, bulk solution assays, and time-lapse TIRF microscopy to probe for functional differences between drebrin isoforms. We found that drebrin A and E are functionally distinct and differ in their ability to inhibit F-actin depolymerization. We showed that both isoforms act as permissive cappers of the barbed end of actin, however, drebrin A has a significantly stronger capping activity, compared to that of the non-neuronal drebrin E. Probing for the molecular level insights on the observed differences revealed that the adult-specific exon in neuronal drebrin A contains an actin binding interface which enhances its permissive capping activity. Strikingly, F-actin decoration by neuronal drebrin A confers significantly stronger resistance to cofilin-mediated severing compared to that of drebrin E. Our results provide novel molecular level insights on functional differences between drebrin isoforms, which deepen our understanding of cytoskeletal regulation in the neuronal context. Our results also helps interpreting the previously reported data related to the silencing or knockout of the neuronal drebrin isoform.

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DBN1

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