Format:
Online-Ressource
ISSN:
1439-7633
Content:
Abstract: Lipoprotein‐binding chaperones mediate intracellular transport of lipidated proteins and determine their proper localisation and functioning. Understanding of the exact structural parameters that determine recognition and transport by different chaperones is of major interest. We have synthesised several lipid‐modified peptides, representative of different lipoprotein classes, and have investigated their binding to the relevant chaperones PDEδ, UNC119a, UNC119b, and galectins‐1 and ‐3. Our results demonstrate that PDEδ recognises S‐isoprenylated C‐terminal peptidic structures but not N‐myristoylated peptides. In contrast, UNC119 proteins bind only mono‐N‐myristoylated, but do not recognise doubly lipidated and S‐isoprenylated peptides at the C terminus. For galectins‐1 and ‐3, neither binding to N‐acylated, nor to C‐terminally prenylated peptides could be determined. These results shed light on the specificity of the chaperone‐mediated cellular lipoprotein transport systems.
In:
volume:16
In:
number:17
In:
year:2015
In:
pages:2460-2465
In:
extent:6
In:
ChemBioChem, Weinheim : Wiley-VCH, [2000]-, 16, Heft 17 (2015), 2460-2465 (gesamt 6), 1439-7633
Language:
English
DOI:
10.1002/cbic.201500355
URN:
urn:nbn:de:101:1-2022122006334957614772
URL:
https://doi.org/10.1002/cbic.201500355
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2022122006334957614772
URL:
https://d-nb.info/1276136706/34
URL:
https://doi.org/10.1002/cbic.201500355
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