Last update 01 Nov 2024

MON1B

Last update 01 Nov 2024

Basic Info

Synonyms

HSRG1, HSV-1 stimulation-related gene 1 protein, HSV-I stimulating-related protein

+ [5]

Introduction-

Drugs associated with MON1B

AAV-delivered CRISPR/Cas9 (Editas Medicine)

Target

MON1B

Mechanism

MON1B agonists [+1]

Active Org.

Editas Medicine, Inc.

Originator Org.

Editas Medicine, Inc.

Active Indication

Keratitis, Herpetic

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with MON1B

100 Translational Medicine associated with MON1B

0 Patents (Medical) associated with MON1B

Literatures (Medical) associated with MON1B

01 Sep 2018·The Journal of ImmunologyQ2 · MEDICINE

Mycobacterial PknG Targets the Rab7l1 Signaling Pathway To Inhibit Phagosome–Lysosome Fusion

Q2 · MEDICINE

Article

Author: Mukhopadhyay, Sangita ; Shrivastva, Rohini ; Pradhan, Gourango

AbstractPhagosome maturation is an important innate defense mechanism of macrophages against bacterial infections. The mycobacterial secretory protein kinase G (PknG), a serine/threonine kinase, is known to block phagosome–lysosome (P–L) fusion, and the kinase activity of PknG appears to be crucial for this. However, the detail mechanisms are not well understood. In the current study, we demonstrate that PknG of Mycobacterium sp. interacts with the human Rab GTPase protein, Rab7l1, but not with other Rab proteins as well as factors like Rabaptin, Rabex5, PI3K3, Mon1a, Mon1b, early endosome autoantigen 1, and LAMP2 that are known to play crucial roles in P–L fusion. The Rab7l1 protein is shown to play a role in P–L fusion during mycobacterial infection, and its absence promotes survival of bacilli inside macrophages. PknG was found to be translocated to the Golgi complex where it interacted with GDP-bound Rab7l1 and blocked transition of inactive Rab7l1-GDP to active Rab7l1-GTP, resulting in inhibition of recruitment of Rab7l1-GTP to bacilli-containing phagosomes, and these processes are dependent on the kinase activity of PknG. Localization of Rab7l1-GTP to phagosomes was found to be critical for the subsequent recruitment of other phago-lysosomal markers like early endosome autoantigen 1, Rab7, and LAMP2 during infection. Thus, by interfering with the Rab7l1 signaling process, PknG prevents P–L fusion and favors bacterial survival inside human macrophages. This study highlights a novel role of Rab7l1 in the phagosomal maturation process and hints at unique strategies of mycobacteria used to interfere with Rab7l1 function to favor its survival inside human macrophages.

01 May 2016·Cell ResearchQ1 · BIOLOGY

Numb regulates vesicular docking for homotypic fusion of early endosomes via membrane recruitment of Mon1b

Q1 · BIOLOGY

Article

Author: Ma, Yifan ; Liu, Xiaoqing ; Qian, Wenyu ; Li, Hongchang ; Liu, Yi ; Jiang, Nan ; Shao, Ximing ; Zhu, Minyan ; Wei, Yanjie ; Yu, Qian ; Ding, Zhihao ; Zhang, Jianchao ; Xu, Zhiheng ; Gui, Linfei ; Jiang, Changan ; Zhang, Lei ; Hong, Yang ; Li, Huashun

Numb is an endocytic protein that plays crucial roles in diverse cellular processes such as asymmetric cell division, cell migration and differentiation. However, the molecular mechanism by which Numb regulates endocytic trafficking is poorly understood. Here, we demonstrate that Numb is a docking regulator for homotypic fusion of early endosomes (EEs). Numb depletion causes clustered but unfused EEs, which can be rescued by overexpressing cytosolic Numb 65 and Numb 71 but not plasma membrane-attached Numb 66 or Numb 72. Time-lapse analysis reveals that paired vesicles tend to tether but not fuse with each other in the absence of Numb. We further show that Numb binds to another docking regulator, Mon1b, and is required for the recruitment of cytosolic Mon1b to the EE membrane. Consistent with this, deletion of Mon1b causes similar defects in EE fusion. Our study thus identifies a novel mechanism by which Numb regulates endocytic sorting by mediating EE fusion.

01 Nov 2013·European Journal of CancerQ1 · MEDICINE

Genetic variants in nuclear factor-kappa B binding sites are associated with clinical outcomes in prostate cancer patients

Q1 · MEDICINE

Article

Author: Chia-Cheng Yu ; Victor C. Lin ; Bo-Ying Bao ; Shin-Hun Juang ; Hong-Zin Lee ; Yung-Chin Lee ; Chao-Yuan Huang ; Shu-Pin Huang ; Te-Ling Lu ; Ta-Yuan Chang

Nuclear factor-kappa B (NF-κB) transcription factors have been suggested to be involved in prostate cancer progression. Activated NF-κB translocates to the nucleus, binds to NF-κB binding sites and regulates target gene expression, leading to the given physiological response. It was hypothesised that the sequence variants in NF-κB binding sites might affect prostate cancer progression. We systematically evaluated 15 single-nucleotide polymorphisms (SNPs) within NF-κB binding sites those were predicted using a genome-wide database in a cohort of 1024 prostate cancer patients. Associations of these SNPs with prostate cancer characteristics and clinical outcomes after radical prostatectomy (RP) for localised disease, and after androgen-deprivation therapy (ADT) for advanced disease were assessed by Kaplan-Meier analysis and Cox regression model. We found that PSMD7 rs2387084 and MYCN rs1429409 were significantly related to earlier onset of prostate cancer and advanced clinical stage, respectively. No SNPs were significantly associated with disease recurrence after RP. Four and three SNPs were notably associated with prostate cancer-specific mortality (PCSM) and all-cause mortality (ACM), respectively, after ADT. LSAMP rs13088089, CCL17 rs223899, PSMD7 rs2387084 and MON1B rs284924 remained the significant predictors for PCSM whilst PSMD7 rs2387084 remained a significant predictor for ACM in multivariate models including clinical predictors. Moreover, we also noted that there were strong effects of the combined genotype on PCSM and patients with a greater number of unfavourable genotypes had a shorter time to PCSM during ADT (P for trend<0.001). It was concluded that SNPs inside NF-κB binding sites might be useful to improve outcome prediction in prostate cancer patients.

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MON1B

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