Request Demo

Last update 08 May 2025

RABGGTB

Last update 08 May 2025

Basic Info

Synonyms

Geranylgeranyl transferase type II subunit beta, Geranylgeranyl transferase type-2 subunit beta, GGTase-II-beta

+ [7]

Introduction

Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.

Drugs associated with RABGGTB

CN118121702

Patent Mining

Target

RABGGTB

Mechanism-

Active Org.

Skin Diseases Hospital, China Academy of Medical Science

Originator Org.

Skin Diseases Hospital, China Academy of Medical Science

Active Indication

Immune System Diseases [+2]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with RABGGTB

100 Translational Medicine associated with RABGGTB

0 Patents (Medical) associated with RABGGTB

Literatures (Medical) associated with RABGGTB

01 Jan 2024·Brain Research Bulletin

RABGGTB plays a critical role in ALS pathogenesis

Article

Author: Dong, Hui ; Liu, Yaling ; Yang, Jing ; Liu, Qi ; Xin, Cheng ; Huo, Jia ; Ma, Haiyang ; Li, Rui

Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease with unknown causes, which mainly affects motor neurons in the anterior horn of the spinal cord, brain stem, and cerebral cortex, also known as motor neuron disease. An important pathological feature of ALS is the formation of aggregates of mutant SOD1 protein, CTF25 of TDP-43, or other abnormal proteins in motor neurons, which require autophagy for degradation. Protein prenylation is known to participate in membrane association and proper localization of proteins. RABGGTB is the β subunit of GGTase II (one of the prenyltransferases) that can regulate autophagy via Rab7 geranylgeranylation. In this study, we overexpressed RABGGTB via lentiviral transfection in NSC34-hSOD1G93A and TDP-43 cells. Overexpression of RABGGTB improved ALS cell proliferation by facilitating autophagosome-lysosome fusion. Furthermore, the abnormal aggregation of SOD1 protein was reduced. This indicates that protein prenylation is important for the proliferation and autophagy of cells autophagy. Enhanced autophagy has been observed in two of the most widely used ALS cell models. These findings indicate the widespread applicability of prenylation in ALS. In summary, overexpression of RABGGTB improved the geranylgeranylation of the Rab7 protein and had a positive effect on cells. These findings provide insights into the development of a novel therapeutic strategy for ALS.

01 Dec 2023·Journal of Periodontology

Prenyltransferase gene expression reveals an essential role of prenylation for the inflammatory response in human gingival fibroblasts

Article

Author: Bachmann, Hagen S. ; Friedmann, Anton ; Diehl, Daniel

AbstractBackgroundPrenyltrasferases (PTases) are a class of enzymes known to be responsible for promoting posttranslational modification at the carboxyl terminus of proteins containing a so‐called CaaX‐motif. The process is responsible for proper membrane localization and the appropriate function of several intracellular signaling proteins. Current research demonstrating the pathomechanistic importance of prenylation in inflammatory illnesses emphasizes the requirement to ascertain the differential expression of PT genes under inflammatory settings, particularly in periodontal disease.MethodsTelomerase‐immortalized human gingival fibroblasts (HGF‐hTert) were cultured and treated with either inhibitors of prenylation (PTI) lonafarnib, tipifarnib, zoledronic acid, or atorvastatin at concentrations of 10 μM in combination with or without 10 μg Porphyromonas gingivalis lipopolysaccharide (LPS) for 24 h. Prenyltransferase genes FNTB, FNTA, PGGT1B, RABGGTA, RABGGTB, and PTAR1 as well as inflammatory marker genes MMP1 and IL1B were detected using quantitative real‐time polymerase chain reaction (RT‐qPCR). Immunoblot and protein immunoassay were used to confirm the results on the protein level.ResultsRT‐qPCR experiments revealed significant upregulation of IL1B, MMP1, FNTA, and PGGT1B upon LPS treatment. PTase inhibitors caused significant downregulation of the inflammatory cytokine expression. Interestingly, FNTB expression was significantly upregulated in response to any PTase inhibitor in combination with LPS, but not upon LPS treatment only, indicating a vital role of protein farnesyltransferase in the proinflammatory signaling cascade.ConclusionsIn this study, distinct PTase gene expression patterns in pro‐inflammatory signaling were discovered. Moreover, PTase inhibiting drugs ameliorated inflammatory mediator expression by a significant margin, indicating that prenylation is a major pre‐requisite for innate immunity in periodontal cells.

01 Jan 2023·Frontiers in aging neuroscience

Protective effects of intrathecal injection of AAV9-RabGGTB-GFP⁺ in SOD1^G93A mice.

Article

Author: Liu, Yaling ; Dong, Hui ; Yang, Jing ; Li, Rui ; Liu, Qi ; Huo, Jia ; Xin, Cheng ; Gao, Tianchu

IntroductionAmyotrophic lateral sclerosis (ALS) is a neurodegenerative disease that widely affects motor neurons of the CNS. About 20% of patients with ALS have familial ALS (fALS). One of the classic models of ALS are SOD1^G93A mice. Misfolded SOD1 protein can be overexpressed in motor neurons, which results in progressive paralysis of the limbs of mice. There is still no effective treatment for ALS. In recent years, the treatment of ALS by regulating autophagy has become a research hotspot. Autophagy obstacles have been confirmed to be one of the early pathological events of ALS. Rab7 is a member of the Ras superfamily and plays a key role in the late stage of autophagy. In our previous studies, we found that prenoylation of Rab7 was inhibited in the ALS model. Prenylation is a post-translational modification in which farnesyl or geranylgeranyl groups are covalently linked to target proteins. Based on these findings, we proposed the novel idea that the regulation of RabGGTB (the β-subunit of RabGGTase) mediated prenylation modification of Rab7, and that this can be used as a prevention and treatment of ALS associated with abnormal protein accumulation.MethodsIn the present study, RabGGTB was overexpressed in mouse spinal cord motoneurons by using adeno-associated virus as vector. Then immunofluorescence quantitative analysis was used for pathological study. The body weight, footprint analysis, the accelerating rotarod test, and neurological deficits score were used to evaluate animal behavior.ResultsOur results show that the protein level of RabGGTB was significantly increased in the lumbar and thoracic regions of spinal cord motoneurons of injected mice. Furthermore, the onset time and survival time of SOD1^G93A mice injected with AAV9-RabGGTB-GFP⁺ were delayed compared with those of mice without overexpression. At the same time, we also observed a decrease in SOD1 misfolded and glial overactivation in the lumbar spinal cord of these SOD1^G93A mice.ConclusionThe findings reported here show that RabGGTB plays a significant role in the pathogenesis of SOD1^G93A mice and with great therapeutic potential for reducing abnormal aggregation of SOD1 in ALS.

Analysis

Perform a panoramic analysis of this field.

view full example data

Hiro LS Researcher

The AI Search Engine Built to Accelerate Biopharma Decisions

Search across billion-scale life sciences data to uncover signals, validate evidence, and act with confidence.

Ask any biopharma research question→

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, Patsnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Discover Synapse Data Servers

Synapse data is now integrated into the PatSnap LS Model Context Protocol (MCP) service. Customize your LLM agent now using our MCP server!

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

RABGGTB

Basic Info

Related

Analysis