Dynactin increases the processivity of the cytoplasmic dynein motor

Nature Cell Biology

Volumn 2, Issue 1, 2000, Pages 20-24

  King, S J ^a   Schroer, T A ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; MOLECULAR MOTOR; POLYSTYRENE;

ARTICLE; BINDING SITE; CONTROLLED STUDY; CYTOPLASM; CYTOSKELETON; ENZYME ACTIVATION; ENZYME BINDING; ENZYME KINETICS; IN VITRO STUDY; IN VIVO STUDY; INTRACELLULAR TRANSPORT; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL;

ADENOSINE TRIPHOSPHATE; ADENOSINETRIPHOSPHATASE; ANIMAL; ANTIBODIES; BINDING SITES; BIOLOGICAL TRANSPORT; CHICK EMBRYO; CYTOPLASM; DYNEIN ATPASE; KINETICS; MICROSPHERES; MICROTUBULE-ASSOCIATED PROTEINS; MICROTUBULES; MOLECULAR MOTORS; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0033789351     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/71338     Document Type: Article

References (35)

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8. Structure and function of dynactin
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12. Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
13. Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
14. The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)
15. CLIPs for organelle-microtubule interactions
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28. Two activators of microtubule-based vesicle transport
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32. Viewing single microtubules by video light microscopy
33. Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor
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