IndraLab

Statements

CYLD deubiquitinates NTRK1. 3 / 3
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"Geetha and collaborators saw that the polyubiquitination of TrkA increases when CYLD is depleted, but no direct evidence of TrkA deubiquitination by CYLD was provided [XREF_BIBR]."
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"In the internalization of the nerve growth factor receptor TrkA, siRNA mediated suppression of CYLD causes sustained TrkA ubiquitination with Lys63 chains (Geetha et al., 2005)."
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"Moreover, additional studies showed that <span class="match term0">CYLD</span> specifically deubiquitinates polyubiquitin chains at K63 of different substrates (e.g., TRAF2 and TRAF6), or tyrosine kinase receptors such as <span class="match term1">TRKA</span>."
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