Parthenolide Inhibits Tubulin Carboxypeptidase Activity

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Parthenolide inhibits tubulin carboxypeptidase activity.

Microtubules are centrally involved in cell division, being the principal components of mitotic spindle. Tubulin, the constituent of microtubules, can be cyclically modified on its alpha-subunit by enzymatic removal of the COOH-terminal tyrosine residue by an ill-defined tubulin carboxypeptidase (TCP) and its readdition by tubulin tyrosine ligase (TTL). We and others have previously shown that ...

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Association of tubulin carboxypeptidase with microtubules in living cells.

Tubulin carboxypeptidase is the enzyme that releases the C-terminal tyrosine from alpha-tubulin, converting tyrosine-terminated (Tyr) to detyrosinated (Glu) tubulin. The present study demonstrates that this enzyme is associated with microtubules in living cells. We extracted cultured cells (COS-7) with Triton X-100 under microtubule-stabilizing conditions and found tubulin carboxypeptidase acti...

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Suppression of tubulin detyrosination by parthenolide recruits the plant-specific kinesin KCH to cortical microtubules

Detyrosination of α-tubulin seems to be conserved in all eukaryotes. However, its biological function in plants has remained obscure. A conserved C-terminal tyrosine is removed by a still unidentified tubulin-tyrosine carboxypeptidase (TTC) and can be religated by a tubulin-tyrosine ligase (TTL). To obtain insight into the still elusive biological function of this detyrosination-tyrosination cy...

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ژورنال

عنوان ژورنال: Cancer Research

سال: 2007

ISSN: 0008-5472,1538-7445

DOI: 10.1158/0008-5472.can-06-3732