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The novel function of Copa in inter-compartmental trafficking of RNA.
SMN directly binds to COPI and moves with survival motor neuron within axons.
In a a large-scale functional screening of mesothelioma cells, the COPA protein was highly expressed in some mesothelioma cell lines but not in a pleural mesothelial cell line.
Reduced RNA editing of COPA gene is associated with psoriasis.
This is the second report of a pathogenic mutation in COPA. The p.Glu241Lys mutation detected in the current Icelandic pedigree is a de novo mutation. The fact that the mutation is absent from 176,040 unrelated individuals but present in two families with affected individuals confirms its role in the pathogenesis of COPA syndrome.
Serum xenin levels of obese patients were higher than in control groups.
COPA variants impair binding to proteins targeted for retrograde Golgi-to-ER transport.
Compared with day workers within the same BMI range, night workers presented a disrupted control of ghrelin (zeige GHRL Proteine) and xenin, associated with behavioural changes in diet and sleep and increased adiposity and related metabolic alterations.
The cell membrane gene SLC4A4 (zeige SLC4A4 Proteine) and the trafficking regulator gene COPA, which also plays an important role in early endosome maturation, were identified for the cellular entry of poly-arginine peptide.
Results show that the interaction between SMN (zeige STMN1 Proteine) and alpha-COP serves an important function in the growth and maintenance of motor neuron processes and may play a significant role in the pathogenesis of Spinal muscular atrophy.
Electron tomography reveals Rab6 is essential to the trafficking of trans-Golgi clathrin and COPI-coated vesicles and the maintenance of Golgi cisternal number
Among ten hepatocellular carcinoma cases with amplicon 1q21-q22, significant gene expression level of JTB (zeige JTB Proteine), SHC1 (zeige SHC1 Proteine), CCT3 (zeige CCT3 Proteine) and COPA in the tumors than the paired adjacent non-malignant liver tissues.
a missense mutation in the coatomer (zeige COPE Proteine) protein complex, subunit alpha (COPA), a gene with previously no known role in pigmentation synthesis, is completely associated with Dominant Red in Holstein dairy cattle.
In eukaryotic cells, protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat proteins (COPs). Seven coat proteins have been identified, and they represent subunits of a complex known as coatomer. The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP, delta-COP, epsilon-COP, and zeta-COP. The alpha-COP, encoded by COPA, shares high sequence similarity with RET1P, the alpha subunit of the coatomer complex in yeast. Also, the N-terminal 25 amino acids of alpha-COP encode the bioactive peptide, xenin, which stimulates exocrine pancreatic secretion and may act as a gastrointestinal hormone. Alternative splicing results in multiple splice forms encoding distinct isoforms.
coatomer protein complex, subunit alpha
, coatomer protein complex alpha subunit
, coatomer protein complex subunit alpha
, Coatomer subunit alpha
, coatomer subunit alpha
, alpha-coat protein
, alpha coat protein