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A more recent version of this article appeared on June 1, 2005
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Submitted on August 6, 2004
Revised on March 2, 2005
Accepted on March 5, 2005
-Tubulin Complex Proteins on Microtubule Nucleation and Catastrophe in Fission Yeast
Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032
Monitoring Editor: David Drubin
Although
-tubulin complexes (
-TuCs) are known as microtubule (MT) nucleators, their function in vivo is still poorly defined. Mto1p (mbo1p/mod20p) is a
-TuC-associated protein that recruits
-TuCs specifically to cytoplasmic MT organizing centers (MTOCs) and interphase MTs (Sawin et al., 2004; Venkatram et al., 2004). Here, we investigated
-TuC function by analyzing MT behavior in mto1
and alp4 (GCP2 homologue) mutants. These cells have free, extralong interphase MTs that exhibit abnormal behaviors such as cycles of growth and breakage, MT sliding, treadmilling, and hyperstability. The plus ends of interphase and spindle MTs grow continuously, exhibiting catastrophe defects which are dependent on the CLIP170 tip1p. The minus ends of interphase MTs exhibit shrinkage and pauses. As mto1
mutants lack cytoplasmic MTOCs, cytoplasmic MTs arise from spindle or other intranuclear MTs that exit the nucleus. Our findings show that mto1p and
-TuCs affect multiple properties of MTs including nucleation, nuclear attachment, plus end catastrophe, and minus end shrinkage.
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