IDENTIFICATION OF A 48-KDA PRENYLATED PROTEIN THAT ASSOCIATES WITH MICROTUBULES AS 2',3'-CYCLIC NUCLEOTIDE 3'-PHOSPHODIESTERASE IN FRTL-5 CELLS

Citation
C. Laezza et al., IDENTIFICATION OF A 48-KDA PRENYLATED PROTEIN THAT ASSOCIATES WITH MICROTUBULES AS 2',3'-CYCLIC NUCLEOTIDE 3'-PHOSPHODIESTERASE IN FRTL-5 CELLS, FEBS letters, 413(2), 1997, pp. 260-264
Citations number
31
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
413
Issue
2
Year of publication
1997
Pages
260 - 264
Database
ISI
SICI code
0014-5793(1997)413:2<260:IOA4PP>2.0.ZU;2-M
Abstract
In an effort to study the nature of tubulin attachment to membranes, w e have previously observed that after blocking prenylation in FRTL-5 t hyroid cells, the microtubules become disconnected from the plasma mem brane region [Bifulco M. et al. (1983) J. Cell. Physiol. 155, 340-348] . In this study we show that several [H-3]mevalonate labeled proteins in FRTL-5 cells associate with membrane and cytoskeleton and, among th ese, we describe the presence of a 48-kDa prenylated protein, identifi ed by immunoprecipitation as 2',3'-cyclic nucleotide 3'-phosphodiester ase (CNP), that associates with microtubules, This latter association persists through several polymerization/depolymerization cycles, where as other prenylated proteins are lost, It is suggested that CNP can be a novel microtubule-associated protein (MAP) and a promising candidat e as a membrane anchor for microtubules. (C) 1997 Federation of Europe an Biochemical Societies.