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Optineurin is an adaptor protein for ubiquitinated substrates in Golgi membrane-associated degradation
by
Lazarou, Michael
, Honda, Shinya
, Arakawa, Satoko
, Shimizu, Shigeomi
, Kawakami, Hideshi
, Oshima, Shigeru
, Okamoto, Ryuichi
, Nibe-Shirakihara, Yoichi
, Sakurai, Hajime Tajima
, Yamaguchi, Hirofumi
, Torii, Satoru
in
13
/ 13/89
/ 13/95
/ 14
/ 14/19
/ 14/28
/ 14/63
/ 38
/ 38/109
/ 631/80/39/2346
/ 631/80/474/582
/ 631/80/642/1525
/ Animals
/ Autophagy
/ Biodegradation
/ Cell cycle
/ Cell Cycle Proteins
/ Degradation
/ Erythrocytes
/ Experiments
/ Golgi apparatus
/ Golgi Apparatus - metabolism
/ HEK293 Cells
/ HeLa Cells
/ Homeostasis
/ Humanities and Social Sciences
/ Humans
/ Intracellular Membranes - metabolism
/ Membrane Transport Proteins - metabolism
/ Membranes
/ Mice
/ Mice, Knockout
/ Mitochondria
/ Mitochondria - metabolism
/ multidisciplinary
/ Proteins
/ Proteolysis
/ Recognition
/ Science
/ Science (multidisciplinary)
/ Signal transduction
/ Substrates
/ Transcription Factor TFIIIA - genetics
/ Transcription Factor TFIIIA - metabolism
/ Ubiquitin
/ Ubiquitination
2025
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Optineurin is an adaptor protein for ubiquitinated substrates in Golgi membrane-associated degradation
by
Lazarou, Michael
, Honda, Shinya
, Arakawa, Satoko
, Shimizu, Shigeomi
, Kawakami, Hideshi
, Oshima, Shigeru
, Okamoto, Ryuichi
, Nibe-Shirakihara, Yoichi
, Sakurai, Hajime Tajima
, Yamaguchi, Hirofumi
, Torii, Satoru
in
13
/ 13/89
/ 13/95
/ 14
/ 14/19
/ 14/28
/ 14/63
/ 38
/ 38/109
/ 631/80/39/2346
/ 631/80/474/582
/ 631/80/642/1525
/ Animals
/ Autophagy
/ Biodegradation
/ Cell cycle
/ Cell Cycle Proteins
/ Degradation
/ Erythrocytes
/ Experiments
/ Golgi apparatus
/ Golgi Apparatus - metabolism
/ HEK293 Cells
/ HeLa Cells
/ Homeostasis
/ Humanities and Social Sciences
/ Humans
/ Intracellular Membranes - metabolism
/ Membrane Transport Proteins - metabolism
/ Membranes
/ Mice
/ Mice, Knockout
/ Mitochondria
/ Mitochondria - metabolism
/ multidisciplinary
/ Proteins
/ Proteolysis
/ Recognition
/ Science
/ Science (multidisciplinary)
/ Signal transduction
/ Substrates
/ Transcription Factor TFIIIA - genetics
/ Transcription Factor TFIIIA - metabolism
/ Ubiquitin
/ Ubiquitination
2025
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Optineurin is an adaptor protein for ubiquitinated substrates in Golgi membrane-associated degradation
by
Lazarou, Michael
, Honda, Shinya
, Arakawa, Satoko
, Shimizu, Shigeomi
, Kawakami, Hideshi
, Oshima, Shigeru
, Okamoto, Ryuichi
, Nibe-Shirakihara, Yoichi
, Sakurai, Hajime Tajima
, Yamaguchi, Hirofumi
, Torii, Satoru
in
13
/ 13/89
/ 13/95
/ 14
/ 14/19
/ 14/28
/ 14/63
/ 38
/ 38/109
/ 631/80/39/2346
/ 631/80/474/582
/ 631/80/642/1525
/ Animals
/ Autophagy
/ Biodegradation
/ Cell cycle
/ Cell Cycle Proteins
/ Degradation
/ Erythrocytes
/ Experiments
/ Golgi apparatus
/ Golgi Apparatus - metabolism
/ HEK293 Cells
/ HeLa Cells
/ Homeostasis
/ Humanities and Social Sciences
/ Humans
/ Intracellular Membranes - metabolism
/ Membrane Transport Proteins - metabolism
/ Membranes
/ Mice
/ Mice, Knockout
/ Mitochondria
/ Mitochondria - metabolism
/ multidisciplinary
/ Proteins
/ Proteolysis
/ Recognition
/ Science
/ Science (multidisciplinary)
/ Signal transduction
/ Substrates
/ Transcription Factor TFIIIA - genetics
/ Transcription Factor TFIIIA - metabolism
/ Ubiquitin
/ Ubiquitination
2025
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Optineurin is an adaptor protein for ubiquitinated substrates in Golgi membrane-associated degradation
Journal Article
Optineurin is an adaptor protein for ubiquitinated substrates in Golgi membrane-associated degradation
2025
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Overview
Golgi membrane-associated degradation (GOMED) is a process that leading to the degradation of proteins that have passed through the
trans
-Golgi membranes upon Golgi stress. GOMED is morphologically similar to autophagy, but the substrates degraded are different, and they thus have different biological roles. Although the substrate recognition mechanism of autophagy has been clarified in detail, that of GOMED is completely unknown. Here we report that GOMED degrades its substrate proteins selectively via optineurin (OPTN), as we found that the degradation of GOMED substrates is s`uppressed by the loss of OPTN. OPTN binds to K33 polyubiquitin-tagged proteins that have passed through the Golgi, which are then incorporated into GOMED structures for eventual degradation. In vivo, GOMED is known to be involved in the removal of mitochondria from erythrocytes, and in Optn-deficient mice, mitochondria are not degraded by GOMED, resulting in the appearance of erythrocytes containing mitochondria. These findings provide insight into the substrate recognition mechanism of GOMED.
Golgi membrane-associated degradation (GOMED) eliminates proteins under Golgi stress, and many substrates carry K33-ubiquitin which is recognized by optineurin to trigger degradation. Without optineurin, defective GOMED leaves mitochondria in red blood cells.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/89
/ 13/95
/ 14
/ 14/19
/ 14/28
/ 14/63
/ 38
/ 38/109
/ Animals
/ Golgi Apparatus - metabolism
/ Humanities and Social Sciences
/ Humans
/ Intracellular Membranes - metabolism
/ Membrane Transport Proteins - metabolism
/ Mice
/ Proteins
/ Science
/ Transcription Factor TFIIIA - genetics
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