CYLD binds polymerized microtubules and directly interacts with HDAC6; inhibition was measured using tubulin deacetylation, not histone deacetylation. These are separable noncatalytic functions of its N-terminal region.

CYLD depletion reduces microtubule dynamics and endothelial-cell polarization and migration. The Rac1 result does not establish Rac1 exchange-factor activity by CYLD.

The abstract supports CYLD-dependent control of Dishevelled K63 ubiquitination and Wnt signaling. It does not identify the exact DVL3 construct supporting the unresolved interaction annotation.

CYLD localizes at centrosomes and basal bodies. The original study distinguishes centrosomal recruitment from catalytic activity in ciliogenesis.

CYLD restricts K63- and Met1-linked ubiquitin on RIPK2 in receptor signaling; this does not imply equivalent editing of every LUBAC substrate.

SPATA2 binds the CYLD USP domain, promotes chain hydrolysis and bridges CYLD to HOIP. CYLD performs deubiquitination, whereas SPATA2 supplies recruitment and activation.

K48 branching can protect K63 linkages from CYLD-mediated cleavage. This is substrate-topology-dependent resistance, not evidence that CYLD hydrolyzes K48 linkages.

Human CYLD has K63 deubiquitinase activity. The disease-associated M719V variant increases activity relative to wild type; mutant phenotypes must not be relabeled as normal protein function.