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Last update 08 May 2025

BET1

Last update 08 May 2025

Basic Info

Synonyms

BET1, Bet1 golgi vesicular membrane trafficking protein, BET1 homolog

+ [2]

Introduction

Required for vesicular transport from the ER to the Golgi complex (PubMed:34779586). Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity).

Drugs associated with BET1

AB500x

Target

BET1

Mechanism

BET1 inhibitors

Active Org.

AevisBio, Inc.

Originator Org.

AevisBio, Inc.

Active Indication

Multiple Myeloma [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

GSK-217

Target

BET1

Mechanism

BET1 inhibitors

Active Org.-

Originator Org.

GSK Plc

Active Indication-

Inactive Indication-

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with BET1

100 Translational Medicine associated with BET1

0 Patents (Medical) associated with BET1

149

Literatures (Medical) associated with BET1

01 Jun 2024·Animal Genetics

The landscape of allelic expression and DNA methylation at the bovine SGCE/PEG10 locus

Article

Author: Chen, Weina ; Zhang, Yinjiao ; Wang, Kun ; Yu, Wenli ; Li, Shujing ; Jin, Lanjie ; Zhang, Cui ; Li, Shijie ; Huo, Haonan

AbstractGenomic imprinting is an epigenetic regulation in mammals in which a small subset of genes is monoallelically expressed dependent on their parental origin. A large imprinted domain, SGCE/PEG10 locus, is located on human chromosome 7q21s and mouse proximal chromosome 6. However, genomic imprinting of bovine SGCE/PEG10 cluster has not been systematically studied. In this study, we investigated allele expression of 14 genes of the SGCE/PEG10 locus in bovine somatic tissues and term placenta using a single nucleotide polymorphism (SNP)‐based sequencing method. In addition to SGCE and PEG10, two conserved paternally expressed genes in human and mice, five other genes (TFPI2, GNG11, ASB4, PON1, and PON3) were paternally expressed. Three genes, BET1, COL1A2, and CASD1, exhibited tissue‐specific monoallelic expression. CALCR showed monoallelic expression in tissues but biallelic expression in the placenta. Three genes, GNGT1, PPP1R9A, and PON2, showed biallelic expression in cattle. Five differentially methylated regions (DMRs) were found to be associated with the allelic expression of TFPI2, COL1A2, SGCE/PEG10, PON3, and ASB4 genes, respectively. The SGCE/PEG10 DMR is a maternally hypermethylated germline DMR, but TFPI2, COL1A2, PON3, and ASB4 DMRs are secondary DMRs. In summary, we identified five novel bovine imprinted genes (GNG11, BET1, COL1A2, CASD1, and PON1) and four secondary DMRs at the SGCE/PEG10 locus.

01 Apr 2024·Journal of Cellular and Molecular Medicine

Proteomic studies in VWA1‐related neuromyopathy allowed new pathophysiological insights and the definition of blood biomarkers

Article

Author: Roos, Andreas ; Hentschel, Andreas ; Ruck, Tobias ; Sickmann, Albert ; Daya, Nassam ; Marina, Adela Della ; Vorgerd, Matthias ; Preusse, Corinna ; Güttsches, Anne‐Katrin ; Gangfuss, Andrea ; Deschauer, Marcus ; Schara‐Schmidt, Ulrike ; Athamneh, Mohammed

AbstractBi‐allelic variants in VWA1, encoding Von Willebrand Factor A domain containing 1 protein localized to the extracellular matrix (ECM), were linked to a neuromuscular disorder with manifestation in child‐ or adulthood. Clinical findings indicate a neuromyopathy presenting with muscle weakness. Given that pathophysiological processes are still incompletely understood, and biomarkers are still missing, we aimed to identify blood biomarkers of pathophysiological relevance: white blood cells (WBC) and plasma derived from six VWA1‐patients were investigated by proteomics. Four proteins, BET1, HNRNPDL, NEFM and PHGDH, known to be involved in neurological diseases and dysregulated in WBC were further validated by muscle‐immunostainings unravelling HNRNPDL as a protein showing differences between VWA1‐patients, healthy controls and patients suffering from neurogenic muscular atrophy and BICD2‐related neuromyopathy. Immunostaining studies of PHGDH indicate its involvement in apoptotic processes via co‐localisation with caspase‐3. NEFM showed an increase in cells within the ECM in biopsies of all patients studied. Plasma proteomics unravelled dysregulation of 15 proteins serving as biomarker candidates among which a profound proportion of increased ones (6/11) are mostly related to antioxidative processes and have even partially been described as blood biomarkers for other entities of neuromuscular disorders before. CRP elevated in plasma also showed an increase in the extracellular space of VWA1‐mutant muscle. Results of our combined studies for the first time describe pathophysiologically relevant biomarkers for VWA1‐related neuromyopathy and suggest that VWA1‐patient derived blood might hold the potential to study disease processes of clinical relevance, an important aspect for further preclinical studies.

30 May 2023·eLife

The Uso1 globular head interacts with SNAREs to maintain viability even in the absence of the coiled-coil domain.

Article

Author: Monterroso, Begoña ; Tagua, Victor G ; Pinar, Mario ; Alonso, Ana ; Arst, Herbert N ; Bravo-Plaza, Ignacio ; Peñalva, Miguel A ; Galindo, Antonio

Uso1/p115 and RAB1 tether ER-derived vesicles to the Golgi. Uso1/p115 contains a globular-head-domain (GHD), a coiled-coil (CC) mediating dimerization/tethering, and a C-terminal region (CTR) interacting with golgins. Uso1/p115 is recruited to vesicles by RAB1. Genetic studies placed Uso1 paradoxically acting upstream of, or in conjunction with RAB1 (Sapperstein et al., 1996). We selected two missense mutations in uso1 resulting in E6K and G540S in the GHD that rescued lethality of rab1-deficient Aspergillus nidulans. The mutations are phenotypically additive, their combination suppressing the complete absence of RAB1, which emphasizes the key physiological role of the GHD. In living hyphae Uso1 recurs on puncta (60 s half-life) colocalizing partially with the Golgi markers RAB1, Sed5, and GeaA/Gea1/Gea2, and totally with the retrograde cargo receptor Rer1, consistent with Uso1 dwelling in a very early Golgi compartment from which ER residents reaching the Golgi recycle back to the ER. Localization of Uso1, but not of Uso1^E6K/G540S, to puncta is abolished by compromising RAB1 function, indicating that E6K/G540S creates interactions bypassing RAB1. That Uso1 delocalization correlates with a decrease in the number of Gea1 cisternae supports that Uso1-and-Rer1-containing puncta are where the protein exerts its physiological role. In S-tag-coprecipitation experiments, Uso1 is an associate of the Sed5/Bos1/Bet1/Sec22 SNARE complex zippering vesicles with the Golgi, with Uso1^E6K/G540S showing a stronger association. Using purified proteins, we show that Bos1 and Bet1 bind the Uso1 GHD directly. However, Bet1 is a strong E6K/G540S-independent binder, whereas Bos1 is weaker but becomes as strong as Bet1 when the GHD carries E6K/G540S. G540S alone markedly increases GHD binding to Bos1, whereas E6K causes a weaker effect, correlating with their phenotypic contributions. AlphaFold2 predicts that G540S increases the binding of the GHD to the Bos1 Habc domain. In contrast, E6K lies in an N-terminal, potentially alpha-helical, region that sensitive genetic tests indicate as required for full Uso1 function. Remarkably, this region is at the end of the GHD basket opposite to the end predicted to interact with Bos1. We show that, unlike dimeric full-length and CTR∆ Uso1 proteins, the GHD lacking the CC/CTR dimerization domain, whether originating from bacteria or Aspergillus extracts and irrespective of whether it carries or not E6K/G540S, would appear to be monomeric. With the finding that overexpression of E6K/G540S and wild-type GHD complement uso1∆, our data indicate that the GHD monomer is capable of providing, at least partially, the essential Uso1 functions, and that long-range tethering activity is dispensable. Rather, these findings strongly suggest that the essential role of Uso1 involves the regulation of SNAREs.

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BET1

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