
IndraLab
Statements
sparser
"Given that the extreme N-terminal CAP-Gly domain of CYLD is essential for its interaction with microtubules 17-19 , the above data indicate that the effect of CYLD on noscapine activity is dependent on the binding of CYLD to microtubules and is independent of its deubiquitinase activity."
sparser
"Although the conserved CAP-GLY domains provide structural basis for the interactions of CYLD with microtubules and many other proteins, an interesting finding is that EB1 containing a known CAP-GLY domain-interacting motif interacts with the C-terminal USP domain of CYLD other than the CAP-GLY domains, implicating a previously unknown role for the USP domain in mediating protein-protein interactions."
sparser
"For example, the cytoskeleton-associated protein-glycine-rich domain mediates the interaction of CYLD with microtubules, whereas calponin homology domain mediates the interaction of EB1 with microtubules. xref , xref , xref In this study, using a combination of taxol-based microtubule isolation and mass spectrometry, we have identified a list of proteins that may potentially associate with microtubules."
sparser
"The DUB CYLD can associate with microtubules through a CAP-Gly domain, regulate their dynamics, and control entry into mitosis ( xref ; xref ; xref ), whereas a ubiquitin C-terminal hydrolase, UCHL1, has also been found associated with microtubules in certain cell types ( xref )."