This title appears in the Scientific Report :
2019
Please use the identifier:
http://hdl.handle.net/2128/23167 in citations.
Please use the identifier: http://dx.doi.org/10.1016/j.bbapap.2018.09.004 in citations.
Positional proteomics for identification of secreted proteoforms released by site-specific processing of membrane proteins
Positional proteomics for identification of secreted proteoforms released by site-specific processing of membrane proteins
Proteolytic processing shapes cellular interactions with the environment. As a pathway of unconventional protein secretion, ectodomain shedding releases soluble proteoforms of membrane-anchored proteins. This can trigger subsequent cleavage within the membrane stub and the release of additional solu...
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Personal Name(s): | Niedermaier, Stefan |
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Huesgen, Pitter (Corresponding author) | |
Contributing Institute: |
Analytik; ZEA-3 |
Published in: | Biochimica et biophysica acta / Proteins and proteomics Proteins and proteomics [...], 1867 (2018) 12, S. 140138 |
Imprint: |
Amsterdam [u.a.]
2018
|
DOI: |
10.1016/j.bbapap.2018.09.004 |
PubMed ID: |
31526490 |
Document Type: |
Journal Article |
Research Program: |
Proteolytic processing in plant stress signal transduction and responses to abiotic stress and pathogen attack Plant Science |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1016/j.bbapap.2018.09.004 in citations.
Proteolytic processing shapes cellular interactions with the environment. As a pathway of unconventional protein secretion, ectodomain shedding releases soluble proteoforms of membrane-anchored proteins. This can trigger subsequent cleavage within the membrane stub and the release of additional soluble fragments to intra- and extracellular environments. Distinct membrane-bound proteases, or sheddases, may cleave the same membrane proteins at different sites. Determination of these precise cleavage sites is important, as differently processed proteoforms may exhibit distinct physiological properties and execute antagonistic paracrine and endocrine signaling functions. Conventional quantitative proteomic approaches reliably identify shed proteoforms, but typically not their termini and are thus not able distinguish between functionally different proteoforms differing only by a few amino acids. Dedicated positional proteomics overcomes this challenge and enables proteome-wide identification of protein N- and C-termini. Here, we review positional proteomics techniques, summarize their application to ectodomain shedding and discuss current challenges and developments. |