Endoplasmic reticulum-associated degradation of glycoproteins in plants
In all eukaryotes the endoplasmic reticulum (ER) has a central role in protein folding and maturation of secretory and membrane proteins. Upon translocation into the ER polypeptides are immediately subjected to folding and modifications involving the formation of disulfide bridges, assembly of subun...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2012-04-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00067/full |
| _version_ | 1818669450174398464 |
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| author | Silvia eHüttner Richard eStrasser |
| author_facet | Silvia eHüttner Richard eStrasser |
| author_sort | Silvia eHüttner |
| collection | DOAJ |
| description | In all eukaryotes the endoplasmic reticulum (ER) has a central role in protein folding and maturation of secretory and membrane proteins. Upon translocation into the ER polypeptides are immediately subjected to folding and modifications involving the formation of disulfide bridges, assembly of subunits to multi-protein complexes and glycosylation. During these processes incompletely folded, terminally misfolded and unassembled proteins can accumulate which endanger the cellular homeostasis and subsequently the survival of cells and tissues. Consequently, organisms have developed a quality control system to cope with this problem and remove the unwanted protein load from the ER by a process collectively referred to as endoplasmic reticulum-associated degradation (ERAD) pathway. Recent studies in Arabidopsis have identified plant ERAD components involved in the degradation of aberrant proteins and evidence was provided for a specific role in abiotic stress tolerance. In this short review we discuss our current knowledge about this important cellular pathway. |
| first_indexed | 2024-12-17T06:52:24Z |
| format | Article |
| id | doaj.art-224d4907796342938058f29910ece94c |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-17T06:52:24Z |
| publishDate | 2012-04-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-224d4907796342938058f29910ece94c2022-12-21T21:59:34ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2012-04-01310.3389/fpls.2012.0006725339Endoplasmic reticulum-associated degradation of glycoproteins in plantsSilvia eHüttner0Richard eStrasser1University of Natural Resources and Life SciencesUniversity of Natural Resources and Life SciencesIn all eukaryotes the endoplasmic reticulum (ER) has a central role in protein folding and maturation of secretory and membrane proteins. Upon translocation into the ER polypeptides are immediately subjected to folding and modifications involving the formation of disulfide bridges, assembly of subunits to multi-protein complexes and glycosylation. During these processes incompletely folded, terminally misfolded and unassembled proteins can accumulate which endanger the cellular homeostasis and subsequently the survival of cells and tissues. Consequently, organisms have developed a quality control system to cope with this problem and remove the unwanted protein load from the ER by a process collectively referred to as endoplasmic reticulum-associated degradation (ERAD) pathway. Recent studies in Arabidopsis have identified plant ERAD components involved in the degradation of aberrant proteins and evidence was provided for a specific role in abiotic stress tolerance. In this short review we discuss our current knowledge about this important cellular pathway.http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00067/fullEndoplasmic ReticulumProtein degradationprotein glycosylationprotein quality controlubiquitin-proteasome |
| spellingShingle | Silvia eHüttner Richard eStrasser Endoplasmic reticulum-associated degradation of glycoproteins in plants Frontiers in Plant Science Endoplasmic Reticulum Protein degradation protein glycosylation protein quality control ubiquitin-proteasome |
| title | Endoplasmic reticulum-associated degradation of glycoproteins in plants |
| title_full | Endoplasmic reticulum-associated degradation of glycoproteins in plants |
| title_fullStr | Endoplasmic reticulum-associated degradation of glycoproteins in plants |
| title_full_unstemmed | Endoplasmic reticulum-associated degradation of glycoproteins in plants |
| title_short | Endoplasmic reticulum-associated degradation of glycoproteins in plants |
| title_sort | endoplasmic reticulum associated degradation of glycoproteins in plants |
| topic | Endoplasmic Reticulum Protein degradation protein glycosylation protein quality control ubiquitin-proteasome |
| url | http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00067/full |
| work_keys_str_mv | AT silviaehuttner endoplasmicreticulumassociateddegradationofglycoproteinsinplants AT richardestrasser endoplasmicreticulumassociateddegradationofglycoproteinsinplants |