Acetylated tubulin associates with the fifth cytoplasmic domain of Na(+)/K(+)-ATPase: possible anchorage site of microtubules to the plasma membrane.
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 (cytoplasmic 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.
Zampar
Guillermo G
GG
Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), UNC-CONICET, Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Córdoba, Argentina.
Chesta
María E
ME
Carbajal
Agustín
A
Chanaday
Natalí L
NL
Díaz
Nicolás M
NM
Casale
César H
CH
Arce
Carlos A
CA
D000107:Acetylation / Q000187:drug effects; D000818:Animals; D001921:Brain / Q000201:enzymology; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D002850:Chromatography, Gel; D003902:Detergents / Q000494:pharmacology; D051379:Mice; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D017434:Protein Structure, Tertiary; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism*; D012995:Solubility / Q000187:drug effects; D014404:Tubulin / Q000378:metabolism*
D003902:Detergents; D014404:Tubulin; D000254:Sodium-Potassium-Exchanging ATPase