ArticleThe Journal of biological chemistry2026
Signal peptide peptidase- and SPP-like 3-dependent shedding of α1,6-fucosyltransferase differentially affects core fucosylation.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha1,6-fucosyltransferase (FUT8) biosynthesizes core fucose on N-glycans, which plays essential roles in various biological processes, including immunity and development. Although FUT8 is a Golgi-resident type II membrane protein, it is also secreted by an unknown mechanism. Here, we demonstrate that signal peptide peptidase (SPP) and signal peptide peptidase-like 3 (SPPL3), members of an intramembrane protease family, both cleave FUT8 for secretion. Knockout of SPP or SPPL3 in cells partially impaired FUT8 secretion, and double KO led to more drastic impairment in secretion, indicating that SPP and SPPL3 independently cleave FUT8. Sequencing analysis revealed that the N terminus of FUT8 in the media was mapped in the stem region, which is far from the expected cleavage site for SPP/SPPL3, suggesting that FUT8 undergoes two-step proteolytic processing, initially by SPP/SPPL3 and subsequently by another protease. Moreover, glycoproteomics suggested that the substrate glycoprotein preference of FUT8 was altered by knocking out SPP or SPPL3, highlighting the importance of FUT8 shedding in core fucosylation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.