Target intelligence / Profile preview

EH domain-containing protein 4 (EHD4)

Target
EHD4
Molecular classification
ATPase, Membrane-associated protein, Dynamin-related protein, Carrier protein, Extracellular matrix protein, Peripheral membrane protein
01

Overview

EH domain-containing protein 4 (EHD4) is a member of the dynamin-related ATPase family involved in cellular membrane trafficking, endocytic recycling, and membrane remodeling in multiple tissues[2][3][4][6][7]. EHD4 binds ATP and associates with lipid membranes, oligomerizing and inducing membrane tubulation to facilitate early endosomal transport[2][4]. In neuronal cells, EHD4 is implicated in the internalization of neurotrophic receptors (TrkA, TrkB) and interacts with proteins such as EHD1, NUMB, PACSIN2, and MICALL1 in the control of membrane protein trafficking[6]. EHD4 is expressed in various tissues, prevalent in heart and detectable in brain, fibroblasts, and cartilage, with functional redundancy alongside other EHD family members[1][6][7]. Disease associations include several cancers and developmental abnormalities[3][6]. No drugs are currently clinically known to directly target EHD4.

Other names
EHD4PAST4HCA10HCA11FKSG7Hepatocellular carcinoma-associated protein 10/11PAST homolog 4EH domain-containing protein 4Ortholog of rat pincher
02

Mechanism of action

Drugs targeting EHD4 would likely modulate endocytic trafficking, membrane remodeling, or receptor internalization pathways; however, no specific drugs are known[3][6].

03

Biological functions

Endocytic recyclingMembrane reorganization/tubulationEarly endosomal transportProtein homooligomerizationCadherin bindingInternalization of receptor proteins (e.g., TrkA, TrkB)Regulation of receptor transport and degradation pathways
04

Disease associations

Cancer (e.g., ovarian, endometrial, hepatocellular carcinoma)Neurodegenerative disease (implicated in axonal growth inhibition and NGF receptor trafficking)Testicular development/male fertility disorders
05

Safety considerations

Functional redundancy may reduce safety risks, but interference with membrane trafficking has potential cellular toxicity risks[6].
06

Biomarkers

Aberrant expression in hepatocellular carcinoma and other cancers (potential biomarker)

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