IndraLab

Statements


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reach
"The interaction between CYLD and HDAC6 was retained in the presence of nocodazole (XREF_FIG), indicating that the interaction between CYLD and HDAC6 does not require intact MTs."

No evidence text available

sparser
"The interaction between CYLD and HDAC6 was retained in the presence of nocodazole ( xref ), indicating that the interaction between CYLD and HDAC6 does not require intact MTs."

sparser
"Furthermore, GST pull-down assays using the N-terminal region of CYLD (GST–CYLD 1–212 ) and the purified form of His-tagged, full-length HDAC6 confirmed an interaction between CYLD and HDAC6 ( xref )."

reach
"CYLD binding to HDAC6 increases alpha-tubulin acetylation."

No evidence text available

reach
"Finally, CYLD also interacts with HDAC6 in the midbody where it regulates the rate of cytokinesis in a deubiquitinase independent manner."

reach
"Furthermore, GST pull-down assays using the N-terminal region of CYLD (GST-CYLD 1-212) and the purified form of His tagged, full-length HDAC6 confirmed an interaction between CYLD and HDAC6 (XREF_FIG)."

reach
"CYLD interacts with p62 directly and CYLD can directly inactivate HDAC6, thereby controlling autophagy [XREF_BIBR]."

sparser
"CYLD binding to HDAC6 increases α -tubulin acetylation."

sparser
"To this end, we immunoprecipitated HDAC6 from Cyld +/+ and Cyld −/− keratinocytes and found that TPA treatment, which was found to induce the interaction of CYLD and HDAC6, did not affect the association of HDAC6 with α-tubulin ( xref )."

sparser
"Finally, CYLD also interacts with HDAC6 in the midbody where it regulates the rate of cytokinesis in a deubiquitinase-independent manner."

sparser
"This hypothesis is supported by our finding that CYLD is unable to bind HDAC6 in the absence of TPA treatment."

sparser
"As expected, only the CYLD 1–212 fragment, which mediates the association of CYLD with HDAC6 ( xref ), was able to inhibit HDAC6 activity and subsequent α-tubulin deacetylation ( xref )."

sparser
"Activation of CYLD increases the levels of acetylated α-tubulin by interaction of the N-terminal domain of CYLD with the catalytic site of HDAC6."

reach
"To this end, we immunoprecipitated HDAC6 from Cyld +/+ and Cyld -/- keratinocytes and found that TPA treatment, which was found to induce the interaction of CYLD and HDAC6, did not affect the association of HDAC6 with alpha-tubulin (XREF_FIG)."

No evidence text available