| Home > Publications Database > Proteolytic ectodomain shedding of membrane proteins in mammals-hardware, concepts, and recent developments. > print |
| 001 | 140123 | ||
| 005 | 20240619102228.0 | ||
| 024 | 7 | _ | |a 10.15252/embj.201899456 |2 doi |
| 024 | 7 | _ | |a pmid:29976761 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC6068445 |2 pmc |
| 024 | 7 | _ | |a 0261-4189 |2 ISSN |
| 024 | 7 | _ | |a 1460-2075 |2 ISSN |
| 024 | 7 | _ | |a altmetric:44715217 |2 altmetric |
| 037 | _ | _ | |a DZNE-2020-06445 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Lichtenthaler, Stefan |0 P:(DE-2719)2181459 |b 0 |e First author |
| 245 | _ | _ | |a Proteolytic ectodomain shedding of membrane proteins in mammals-hardware, concepts, and recent developments. |
| 260 | _ | _ | |a Hoboken, NJ [u.a.] |c 2018 |b Wiley |
| 264 | _ | 1 | |3 online |2 Crossref |b EMBO |c 2018-07-05 |
| 264 | _ | 1 | |3 print |2 Crossref |b EMBO |c 2018-08-01 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1718785302_8364 |2 PUB:(DE-HGF) |x Review Article |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Proteolytic removal of membrane protein ectodomains (ectodomain shedding) is a post-translational modification that controls levels and function of hundreds of membrane proteins. The contributing proteases, referred to as sheddases, act as important molecular switches in processes ranging from signaling to cell adhesion. When deregulated, ectodomain shedding is linked to pathologies such as inflammation and Alzheimer's disease. While proteases of the 'a disintegrin and metalloprotease' (ADAM) and 'beta-site APP cleaving enzyme' (BACE) families are widely considered as sheddases, in recent years a much broader range of proteases, including intramembrane and soluble proteases, were shown to catalyze similar cleavage reactions. This review demonstrates that shedding is a fundamental process in cell biology and discusses the current understanding of sheddases and their substrates, molecular mechanisms and cellular localizations, as well as physiological functions of protein ectodomain shedding. Moreover, we provide an operational definition of shedding and highlight recent conceptual advances in the field. While new developments in proteomics facilitate substrate discovery, we expect that shedding is not a rare exception, but rather the rule for many membrane proteins, and that many more interesting shedding functions await discovery. |
| 536 | _ | _ | |a 342 - Disease Mechanisms and Model Systems (POF3-342) |0 G:(DE-HGF)POF3-342 |c POF3-342 |f POF III |x 0 |
| 542 | _ | _ | |i 2018-07-05 |2 Crossref |u http://onlinelibrary.wiley.com/termsAndConditions#vor |
| 542 | _ | _ | |i 2018-07-05 |2 Crossref |u http://doi.wiley.com/10.1002/tdm_license_1.1 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a Membrane Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Amyloid Precursor Protein Secretases |0 EC 3.4.- |2 NLM Chemicals |
| 650 | _ | 7 | |a Aspartic Acid Endopeptidases |0 EC 3.4.23.- |2 NLM Chemicals |
| 650 | _ | 7 | |a BACE1 protein, human |0 EC 3.4.23.46 |2 NLM Chemicals |
| 650 | _ | 7 | |a ADAM Proteins |0 EC 3.4.24.- |2 NLM Chemicals |
| 650 | _ | 2 | |a ADAM Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Amyloid Precursor Protein Secretases: metabolism |2 MeSH |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Aspartic Acid Endopeptidases: metabolism |2 MeSH |
| 650 | _ | 2 | |a Cell Membrane: metabolism |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Membrane Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Protein Domains: physiology |2 MeSH |
| 650 | _ | 2 | |a Protein Processing, Post-Translational: physiology |2 MeSH |
| 650 | _ | 2 | |a Proteolysis |2 MeSH |
| 650 | _ | 2 | |a Signal Transduction |2 MeSH |
| 700 | 1 | _ | |a Lemberg, Marius K |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Fluhrer, Regina |0 P:(DE-2719)2000007 |b 2 |
| 773 | 1 | 8 | |a 10.15252/embj.201899456 |b : EMBO, 2018-07-05 |n 15 |3 journal-article |2 Crossref |t The EMBO Journal |v 37 |y 2018 |x 0261-4189 |
| 773 | _ | _ | |a 10.15252/embj.201899456 |g Vol. 37, no. 15 |0 PERI:(DE-600)1467419-1 |n 15 |q 37:15 |p e99456 |t The EMBO journal |v 37 |y 2018 |x 0261-4189 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6068445 |
| 856 | 4 | _ | |u https://pub.dzne.de/record/140123/files/DZNE-2020-06445_Restricted.pdf |
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| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 0 |6 P:(DE-2719)2181459 |
| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 2 |6 P:(DE-2719)2000007 |
| 913 | 1 | _ | |a DE-HGF |b Gesundheit |l Erkrankungen des Nervensystems |1 G:(DE-HGF)POF3-340 |0 G:(DE-HGF)POF3-342 |3 G:(DE-HGF)POF3 |2 G:(DE-HGF)POF3-300 |4 G:(DE-HGF)POF |v Disease Mechanisms and Model Systems |x 0 |
| 914 | 1 | _ | |y 2018 |
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| 920 | 1 | _ | |0 I:(DE-2719)1110000-2 |k AG Fluhrer |l Signal Peptide Peptidases as Models for γ-Secretase |x 1 |
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| 999 | C | 5 | |9 -- missing cx lookup -- |a 10.1080/14728222.2016.1182990 |2 Crossref |o 10.1080/14728222.2016.1182990 |
| 999 | C | 5 | |9 -- missing cx lookup -- |a 10.1038/ncomms14740 |2 Crossref |o 10.1038/ncomms14740 |
| 999 | C | 5 | |9 -- missing cx lookup -- |a 10.1128/MCB.26.9.3353-3364.2006 |2 Crossref |o 10.1128/MCB.26.9.3353-3364.2006 |
| 999 | C | 5 | |9 -- missing cx lookup -- |a 10.1074/jbc.M112.377465 |2 Crossref |o 10.1074/jbc.M112.377465 |
| 999 | C | 5 | |9 -- missing cx lookup -- |a 10.1016/j.biopsych.2016.12.023 |2 Crossref |o 10.1016/j.biopsych.2016.12.023 |
| 999 | C | 5 | |9 -- missing cx lookup -- |a 10.1016/j.bbamcr.2017.07.001 |2 Crossref |o 10.1016/j.bbamcr.2017.07.001 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|