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Distinguishing between retention signals and degrons acting in ERAD
Year:
2007
Source of publication :
Journal of Cell Science
Authors :
Charuvi, Dana
;
.
Volume :
120
Co-Authors:
Shapira, I., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Charuvi, D., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel, The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
Elkabetz, Y., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel, Laboratory of Stem Cell and Tumor Biology, Division of Neurosurgery and Developmental Biology Program, Sloan-Kettering Institute, New York, NY, United States
Hirschberg, K., Department of Pathology, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel
Bar-Nun, S., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Facilitators :
From page:
4377
To page:
4387
(
Total pages:
11
)
Abstract:
Endoplasmic reticulum-associated degradation (ERAD) eliminates aberrant proteins from the secretory pathway. Such proteins are retained in the endoplasmic reticulum and targeted for degradation by the ubiquitin-proteasome system. Cis-acting motifs can function in ERAD as retention signals, preventing vesicular export from the endoplasmic reticulum, or as degrons, targeting proteins for degradation. Here, we show that μstp, the C-terminal 20-residue tailpiece of the secretory IgM μs heavy chain, functions both as a portable retention signal and as an ERAD degron. Retention of μstp fusions of secreted versions of thyroid peroxidase and yellow fluorescent protein in the endoplasmic reticulum requires the presence of the penultimate cysteine of μstp. In its role as a portable degron, the μstp targets the retained proteins for ERAD but does not serve as an obligatory ubiquitin-conjugation site. Abolishing μstp glycosylation accelerates the degradation of both μstpCys-fused substrates, yet absence of the N-glycan eliminates the requirement for the penultimate cysteine in the retention and degradation of the unglycosylated yellow fluorescent protein. Hence, the dual role played by the μstpCys motif as a retention signal and as a degron can be attributed to distinct elements within this sequence.
Note:
Related Files :
carboxy terminal sequence
cis acting element
Degrons
HeLa cells
Polysaccharides
proteins
thyroid peroxidase
Show More
Related Content
More details
DOI :
10.1242/jcs.011247
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
31334
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:01
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Scientific Publication
Distinguishing between retention signals and degrons acting in ERAD
120
Shapira, I., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Charuvi, D., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel, The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
Elkabetz, Y., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel, Laboratory of Stem Cell and Tumor Biology, Division of Neurosurgery and Developmental Biology Program, Sloan-Kettering Institute, New York, NY, United States
Hirschberg, K., Department of Pathology, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel
Bar-Nun, S., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Distinguishing between retention signals and degrons acting in ERAD
Endoplasmic reticulum-associated degradation (ERAD) eliminates aberrant proteins from the secretory pathway. Such proteins are retained in the endoplasmic reticulum and targeted for degradation by the ubiquitin-proteasome system. Cis-acting motifs can function in ERAD as retention signals, preventing vesicular export from the endoplasmic reticulum, or as degrons, targeting proteins for degradation. Here, we show that μstp, the C-terminal 20-residue tailpiece of the secretory IgM μs heavy chain, functions both as a portable retention signal and as an ERAD degron. Retention of μstp fusions of secreted versions of thyroid peroxidase and yellow fluorescent protein in the endoplasmic reticulum requires the presence of the penultimate cysteine of μstp. In its role as a portable degron, the μstp targets the retained proteins for ERAD but does not serve as an obligatory ubiquitin-conjugation site. Abolishing μstp glycosylation accelerates the degradation of both μstpCys-fused substrates, yet absence of the N-glycan eliminates the requirement for the penultimate cysteine in the retention and degradation of the unglycosylated yellow fluorescent protein. Hence, the dual role played by the μstpCys motif as a retention signal and as a degron can be attributed to distinct elements within this sequence.
Scientific Publication
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