Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation

Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately delivered to the proteasome for degradation. It...

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Veröffentlicht in:	PloS one 2012-05, Vol.7 (5), p.e36542-e36542
Hauptverfasser:	Blount, Jessica R, Burr, Aaron A, Denuc, Amanda, Marfany, Gemma, Todi, Sokol V
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer's disease Animals Biology Cell division Cercopithecus aethiops COS Cells Degradation Endoplasmic reticulum Endoplasmic Reticulum - enzymology Endoplasmic Reticulum - genetics Endoplasmic Reticulum-Associated Degradation - physiology Enzymes Genomes HEK293 Cells Humans Ligases Medicine Microscopy Mutation Neurology Neurotoxicity Pathogenesis Pharmacology Post-translational modifications Protease Proteases Proteasome Endopeptidase Complex - genetics Proteasome Endopeptidase Complex - metabolism Proteasomes Proteins Proteolysis Quality control Quality management Substrates Ubiquitin Ubiquitin Thiolesterase - genetics Ubiquitin Thiolesterase - metabolism Ubiquitin-protein ligase Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitin-specific proteinase Ubiquitinated Proteins - genetics Ubiquitinated Proteins - metabolism Ubiquitination Ubiquitination - physiology
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