Acetylated tubulin associates with the fifth cytoplasmic domain of Na /K -ATPase: possible anchorage site of microtubules to the plasma membrane

作者：Zampar Guillermo G; Chesta Maria E; Carbajal Agustin; Chanaday Natali L; Diaz Nicols M; Casale Csar H; Arce Carlos A^*

来源：Biochemical Journal, 2009, 422(1): 129-137.

DOI：10.1042/BJ20082410

• acetylated tubulin-binding domain
• acetylation
• cytoskeleton
• P-type ATPase (P-ATPase)
• post-translational modification
• sodium pump

We showed previously that NKA (Na -/K -ATPase) interacts with acetylated tubulin resulting in inhibition of its catalytic activity. In the present work we determined that membrane-acetylated tubulin, in the presence of detergent, behaves as an entity of discrete molecular mass (320-400 kDa during molecular exclusion chromatography. We also found that microtubules assembled in vitro are able to bind to NKA when incubated with a detergent-solubilized membrane preparation, and that isolated native microtubules have associated NKA. Furthermore, we determined that CD5 (cyloplasmic domain 5 of NKA) is capable of interacting with acetylated tubulin. Taken together. Our results are consistent with the idea that NKA may act as a microtubule-plasma membrane anchorage site through an interaction between acetylated tubulin and CD5.

• 出版日期2009-8-15