In:
The EMBO Journal, EMBO, Vol. 33, No. 24 ( 2014-12-17), p. 2890-2905
Abstract:
image SPPL 3 is a highly conserved eukaryotic intramembrane‐cleaving Gx GD ‐type aspartyl protease of undefined function. We show that SPPL 3 liberates medial / trans ‐Golgi glycosyltransferases from their N‐terminal membrane anchors to regulate the intracellular pool of active Golgi glycosyltransferases and the extent of N‐glycan decoration of cellular glycoproteins. Loss of SPPL3 in vitro and in vivo is associated with more extensive N‐glycosylation. Overexpression of active SPPL3, but not of an inactive mutant, leads to less extensive N‐glycosylation. Constitutive secretion of Golgi glycosyltransferases such as GnT‐V, β3GnT1 and β4GalT1 is dependent on cellular SPPL3 activity. SPPL3‐dependent GnT‐V endoproteolysis occurs close to GnT‐V's predicted transmembrane domain. Changes in SPPL3 expression strongly affect intracellular glycosyltransferase levels, explaining the observed alterations in N‐glycan composition.
Type of Medium:
Online Resource
ISSN:
0261-4189
,
1460-2075
DOI:
10.15252/embj.201488375
Language:
English
Publisher:
EMBO
Publication Date:
2014
detail.hit.zdb_id:
1467419-1
detail.hit.zdb_id:
586044-1
SSG:
12
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