Ubiquitination and Its Role in Platelet Function – Platelets Journal
Platelets Journal shared a post on LinkedIn about a recent article by M. Allet et al, adding:
“New review available in Platelets
‘Mechanistic insights into ubiquitin mediated regulation of platelet function’ by M. Allet, et al. (2026).
Platelets lack transcriptional capacity, so they may rely more than nucleated cells on post-translational modification.
Mugthalana Allet and colleagues review ubiquitination: the enzymes platelets carry, what gets ubiquitinated, and the existing gaps in the literature.
Platelets express both E1 enzymes, at least thirteen E2s, thirty two E3 ligases, fifteen deubiquitinases and the full 26S proteasome, with at least 70 ubiquitin enzymes shared with mouse platelets.
Furthermore, this machinery is active: resting platelets carry 1,643 ubiquitinated peptides from 691 proteins, over half doubling after GPVI stimulation, across K6, K11, K27, K48 and K63 linkages.
Mechanistically, the Cbl family exerts both positive and negative control of GPVI signalling, with c Cbl modulating Syk non degradatively; LUBAC ubiquitinates NEMO in non genomic NF κB signalling; USP25 sustains Talin 1 by stripping K48 chains, its loss impairing integrin function; and proteasome inhibition blocks αIIbβ3 activation and halves platelet half life.
Clinically, this machinery cuts both ways: proteasome inhibitors and IMiDs are associated with thrombocytopenia, with IMiDs also carrying thromboembolic risk, while PROTACs, which recruit E3 ligases to degrade a chosen target, have degraded BTK and TEC in platelets and inhibited platelet function, pointing toward more selective antiplatelet agents.”
Title: Mechanistic insights into ubiquitin-mediated regulation of platelet function
Authors: M. Allet, J. D. Humphries, K. M. Naseem, A. J. Unsworth
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