2′,3′-Cyclic nucleotide 3′-phosphodiesterase: A membrane-bound, microtubule-associated protein and membrane anchor for tubulin

Author:

Bifulco Maurizio1,Laezza Chiara1,Stingo Stefania1,Wolff J.1

Affiliation:

1. Dipartimento di Scienze Farmaceutiche, Università di Salerno, 84084 Fisciano, Salerno, Italy; Centro di Studio per la Endocrinologia e l'Oncologia Sperimentale G. Salvatore del Consiglio Nazionale delle Ricerche, Dipartimento di Biologia e Patologia Cellulare e Molecolare “L. Califano,” Università “Federico II,” 80131 Naples, Italy; and Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892

Abstract

2′,3′-Cyclic nucleotide-3′-phosphodiesterase (CNP) is firmly associated with tubulin from brain tissue and FRTL-5 thyroid cells as demonstrated by copolymerization with microtubules through several warm/cold cycles, the presence of CNP activity in purified tubulin preparations, and identical behavior during various extraction procedures. CNP acts as a microtubule-associated protein in promoting microtubule assembly at low mole ratios. This activity resides in the C terminus of the enzyme, which, by itself, promotes microtubule assembly at higher mole ratios. Phosphorylation of CNP interferes with its assembly-promoting activity, as does deletion of the C terminus, which leads to abnormal microtubule distribution in the cell. Submembranous colocalization of the proteins and CNP-dependent microtubule organization suggest that CNP is a membrane-bound microtubule-associated protein that can link tubulin to membranes and may regulate cytoplasmic microtubule distribution.

Publisher

Proceedings of the National Academy of Sciences

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