Target intelligence / Profile preview

Coatomer subunit beta 1 (COPB1)

Target
COPB1
Molecular classification
Other (Coat protein complex subunit), Component of the COPI vesicle coatomer complex
01

Overview

Coatomer subunit beta 1 (COPB1) is a protein encoded by the COPB1 gene and acts as a core component of the coat protein complex I (COPI), a cytosolic complex mediating vesicular transport between the endoplasmic reticulum and the Golgi apparatus[1][2][3][5]. COPB1 binds dilysine motifs and participates in budding and fusion of non-clathrin-coated vesicles essential for retrograde trafficking of proteins and lipids, Golgi membrane dynamics, and compartmentalization within the early secretory pathway[1][2][5]. It also plays roles in lipid droplet homeostasis, autophagy, and proper degradation of specific proteins, being vital for cellular homeostasis and organelle function[1][5]. Disease mutations can cause congenital disorders such as Baralle-Macken syndrome and primary bone dysplasia[1]. As a ubiquitous and essential intracellular transport protein, COPB1 is not considered a direct therapeutic target, and no approved drugs or biomarkers are associated with it[1][5].

Other names
COPB1COPBCoatomer subunit betaBeta-COPBeta-coat proteinBARMACSCOPI coat complex subunit beta 1beta coat proteincoatomer protein complex subunit beta 1MSTP026beta-cop
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Biological functions

Mediates retrograde transport from the Golgi apparatus to the endoplasmic reticulum (ER)Involved in Golgi disassembly and reassembly during the cell cycleEssential for proper organelle compartmentalization and vesicular traffickingRegulates lipid homeostasis and lipid droplet dynamicsFacilitates transport and translation of specific mRNAs, including kappa-type opioid receptor mRNAAutophagy modulation and early endosome functionInvolved in degradation of certain cellular targets (e.g., MHC class I antigens)
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Disease associations

Baralle-Macken syndromePrimary bone dysplasiaOther (rare genetic disorders; possible implication in vesicular transport-related diseases)
04

Safety considerations

Essential cellular function: complete inhibition is likely toxic or lethal to cellsDisruption can affect multiple trafficking and organelle processes, with wide-ranging cellular consequences

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