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

Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1807-12. doi: 10.1073/pnas.042678799. Epub 2002 Feb 12.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 2',3'-Cyclic-Nucleotide Phosphodiesterases / chemistry*
  • 2',3'-Cyclic-Nucleotide Phosphodiesterases / metabolism
  • 2',3'-Cyclic-Nucleotide Phosphodiesterases / physiology*
  • Amino Acid Sequence
  • Animals
  • Brain / cytology
  • Cell Line
  • Cell Membrane / metabolism
  • Cytoplasm / chemistry
  • Cytoplasm / metabolism
  • DNA, Complementary / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Genetic Vectors
  • Glutathione Transferase / metabolism
  • Green Fluorescent Proteins
  • Immunoblotting
  • Luminescent Proteins / metabolism
  • Microscopy, Fluorescence
  • Microtubules / chemistry
  • Microtubules / metabolism
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Binding
  • Protein Structure, Tertiary
  • Rats
  • Recombinant Fusion Proteins / metabolism
  • Subcellular Fractions
  • Thyroid Gland / cytology
  • Time Factors
  • Transfection
  • Tubulin / chemistry*
  • Tubulin / metabolism

Substances

  • DNA, Complementary
  • Luminescent Proteins
  • Recombinant Fusion Proteins
  • Tubulin
  • Green Fluorescent Proteins
  • Glutathione Transferase
  • 2',3'-Cyclic-Nucleotide Phosphodiesterases