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In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain
- Source :
- Journal of Cell Science. 120:4093-4098
- Publication Year :
- 2007
- Publisher :
- The Company of Biologists, 2007.
-
Abstract
- Intracellular movement is a fundamental property of all cell types. Many organelles and molecules are actively transported throughout the cytoplasm by molecular motors, such as the dimeric type V myosins. These possess a long neck, which contains an IQ motif, that allow it to make 36-nm steps along the actin polymer. Live cell imaging of the fission yeast type V myosin Myo52 reveals that the protein moves rapidly throughout the cytoplasm. Here, we describe analysis of this movement and have established that Myo52 moves long distances on actin filaments in an ATP-dependent manner at ∼0.5 μm/second. Myo51 and the microtubule cytoskeleton have no discernable role in modulating Myo52 movements, whereas rigour mutations in Myo52 abrogated its movement. We go on to show that, although dimerisation is required for Myo52 movement, deleting its neck has no discernable affect on Myo52 function or velocity in vivo.
- Subjects :
- Amino Acid Motifs
Green Fluorescent Proteins
Molecular Sequence Data
Myosin Type V
Biology
Adenosine Triphosphate
Live cell imaging
Lectins
Two-Hybrid System Techniques
Schizosaccharomyces
Organelle
Myosin
Molecular motor
Amino Acid Sequence
Actin
Fluorescent Dyes
Microscopy, Video
Rhodamines
Cell Biology
biology.organism_classification
Actins
Protein Structure, Tertiary
Cell biology
Actin Cytoskeleton
Kinetics
Microscopy, Fluorescence
Cytoplasm
Mutation
Schizosaccharomyces pombe
Dimerization
Intracellular
Subjects
Details
- ISSN :
- 14779137 and 00219533
- Volume :
- 120
- Database :
- OpenAIRE
- Journal :
- Journal of Cell Science
- Accession number :
- edsair.doi.dedup.....731341da6867e169f005d7892acd6034
- Full Text :
- https://doi.org/10.1242/jcs.012468