Identification of a 48‐kDa prenylated protein that associates with microtubules as 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase in FRTL‐5 cells

FEBS Letters

Bifulco, Maurizio¹  Wolff, J²  Laezza, Chiara¹ 

[1] CEOS/CNR and Dipartimento di Biologia e Patologia Cellulare e Molecolare `L. Califano', Università `Federico II', via S. Pansini 5, 80131 Napoli, Italy;Laboratory of Biochemical Pharmacology, NIDDK, NIH, Bethesda, MD20892, USA

关键词: 2′;    3′-Cyclic nucleotide 3′-phosphodiesterase;    Microtubule-associated proteins;    Prenylation;    FRTL-5 thyroid cells;    CNP1;    2;    2′;    3′-cyclic nucleotide 3′-phosphodiesterase 1 and 2;    MAP;    microtubule-associated proteins;    MVA;    mevalonate;    pCNP7;    CNP1 cDNA;    PBS;    phosphate buffered saline;    Pipes;    piperazine N;    N-bis(2-ethane sulfonic acid);    PMSF;    phenylmethyl sulfonyl fluoride;    DTT;    dithiothreitol;   

DOI  :  10.1016/S0014-5793(97)00924-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In an effort to study the nature of tubulin attachment to membranes, we have previously observed that after blocking prenylation in FRTL-5 thyroid cells, the microtubules become disconnected from the plasma membrane region [Bifulco M. et al. (1983) J. Cell. Physiol. 155, 340–348]. In this study we show that several [³H]mevalonate labeled proteins in FRTL-5 cells associate with membrane and cytoskeleton and, among these, we describe the presence of a 48-kDa prenylated protein, identified by immunoprecipitation as 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNP), that associates with microtubules. This latter association persists through several polymerization/depolymerization cycles, whereas other prenylated proteins are lost. It is suggested that CNP can be a novel microtubule-associated protein (MAP) and a promising candidate as a membrane anchor for microtubules.

【 授权许可】

Unknown