Stathmin-Tubutin Interaction Gradients in Motile and Mitotic Cells

Science

Volumn 303, Issue 5665, 2004, Pages 1862-1866

  Niethammer, Philipp ^a   Bastiaens, Philippe ^a   Karsenti, Eric ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSENSORS; ENERGY TRANSFER; FLUORESCENCE; RESONANCE;

MICROTUBULES; PHOSPHORYLATION;

CELLS;

STATHMIN; TUBULIN; BACTERIAL PROTEIN; CITRINE PROTEIN, BACTERIA; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; MICROTUBULE PROTEIN; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHOPROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PHOTOPROTEIN; STATHMIN PROTEIN, XENOPUS; XENOPUS PROTEIN;

BIOLOGY;

ARTICLE; BIOSENSOR; CELL INTERACTION; CELL MOTILITY; CYTOSKELETON; FLUORESCENCE RESONANCE ENERGY TRANSFER; INTERPHASE; MICROFILAMENT; MICROTUBULE ASSEMBLY; MITOSIS; MOLECULAR DYNAMICS; MONITORING; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; ANIMAL; BINDING SITE; CELL LINE; CELL MOTION; CHROMOSOME; CYTOSOL; GENETIC TRANSFECTION; GENETICS; METABOLISM; MICROTUBULE; MITOSIS SPINDLE; MUTATION; PHOSPHORYLATION; PROTEIN BINDING; SWINE; ULTRASTRUCTURE; XENOPUS;

ANIMALS; BACTERIAL PROTEINS; BINDING SITES; CELL LINE; CELL MOVEMENT; CHROMOSOMES; CYTOSOL; FLUORESCENCE RESONANCE ENERGY TRANSFER; GREEN FLUORESCENT PROTEINS; INTERPHASE; LUMINESCENT PROTEINS; MICROTUBULE PROTEINS; MICROTUBULES; MITOSIS; MITOTIC SPINDLE APPARATUS; MUTATION; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN BINDING; RECOMBINANT FUSION PROTEINS; STATHMIN; SWINE; TETRADECANOYLPHORBOL ACETATE; TRANSFECTION; TUBULIN; XENOPUS; XENOPUS PROTEINS;

EID: 1642322097     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1094108     Document Type: Article

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33. We thank R. Heald for the kind gift of the stathmin mutants, T. Stauber for comments on the manuscript, T. Zimmermann and J. Rietdorf for help with microscopy, and V. Georget for helpful advice concerning doning procedures. We also thank I. Amal for initial trials on the detection of stathmin-tubulin interactions.