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The microtubule-dependent motor centromere-associated protein E (CENP-E) is an integral component of kinetochore corona fibers that link centromeres to spindle microtubules.

Yao X, Anderson KL, Cleveland DW - J. Cell Biol. (1997)

Bottom Line: Centromere-associated protein E (CENP-E) is a kinesin-related microtubule motor protein that is essential for chromosome congression during mitosis.In congressing chromosomes, CENP-E is preferentially associated with (or accessible at) the stretched, leading kinetochore known to provide the primary power for chromosome movement.Taken together, this evidence strongly supports a model in which CENP-E functions in congression to tether kinetochores to the disassembling microtubule plus ends.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Cell Biology, Ludwig Institute for Cancer Research, School of Medicine, University of California, La Jolla, CA 92093-0660, USA.

ABSTRACT
Centromere-associated protein E (CENP-E) is a kinesin-related microtubule motor protein that is essential for chromosome congression during mitosis. Using immunoelectron microscopy, CENP-E is shown to be an integral component of the kinetochore corona fibers that tether centromeres to the spindle. Immediately upon nuclear envelope fragmentation, an associated plus end motor trafficks cytoplasmic CENP-E toward chromosomes along astral microtubules that enter the nuclear volume. Before or concurrently with initial lateral attachment of spindle microtubules, CENP-E targets to the outermost region of the developing kinetochores. After stable attachment, throughout chromosome congression, at metaphase, and throughout anaphase A, CENP-E is a constituent of the corona fibers, extending at least 50 nm away from the kinetochore outer plate and intertwining with spindle microtubules. In congressing chromosomes, CENP-E is preferentially associated with (or accessible at) the stretched, leading kinetochore known to provide the primary power for chromosome movement. Taken together, this evidence strongly supports a model in which CENP-E functions in congression to tether kinetochores to the disassembling microtubule plus ends.

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CENP-E cross-links the interzonal microtubules during  telophase. HeLa cells were processed as described in Fig. 2. (A)  Low magnification view of a late telophase HeLa cell. Lamin  deposition to reform nuclei is partially complete. (B) Magnified  view of boxed area in A shows that CENP-E is located along and/ or between the interzonal microtubules (boxed). (C) Higher magnification of interzonal microtubules shows that gold particles are  primarily located between the microtubule bundles. Bars: (A) 2  μm; (B) 500 nm; (C) 90 nm.
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Figure 8: CENP-E cross-links the interzonal microtubules during telophase. HeLa cells were processed as described in Fig. 2. (A) Low magnification view of a late telophase HeLa cell. Lamin deposition to reform nuclei is partially complete. (B) Magnified view of boxed area in A shows that CENP-E is located along and/ or between the interzonal microtubules (boxed). (C) Higher magnification of interzonal microtubules shows that gold particles are primarily located between the microtubule bundles. Bars: (A) 2 μm; (B) 500 nm; (C) 90 nm.

Mentions: To test if detectable CENP-E remains at telophase centromeres, when the functional kinetochores are disassembled, we examined cells in telophase. Fig. 8 A displays a cell in which chromosomes are decondensing and a nuclear lamina has begun to reform around the DNA. No CENP-E was found chromosome associated. Rather, CENP-E was restricted to bundles of antiparallel microtubules in the midzone. For example (Fig. 8 B), in each of five microtubule bundles formed by antiparallel microtubules, CENP-E was found microtubule associated, but only in the electron dense region of overlapping microtubule plus ends (Fig. 8 C).


The microtubule-dependent motor centromere-associated protein E (CENP-E) is an integral component of kinetochore corona fibers that link centromeres to spindle microtubules.

Yao X, Anderson KL, Cleveland DW - J. Cell Biol. (1997)

CENP-E cross-links the interzonal microtubules during  telophase. HeLa cells were processed as described in Fig. 2. (A)  Low magnification view of a late telophase HeLa cell. Lamin  deposition to reform nuclei is partially complete. (B) Magnified  view of boxed area in A shows that CENP-E is located along and/ or between the interzonal microtubules (boxed). (C) Higher magnification of interzonal microtubules shows that gold particles are  primarily located between the microtubule bundles. Bars: (A) 2  μm; (B) 500 nm; (C) 90 nm.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2139792&req=5

Figure 8: CENP-E cross-links the interzonal microtubules during telophase. HeLa cells were processed as described in Fig. 2. (A) Low magnification view of a late telophase HeLa cell. Lamin deposition to reform nuclei is partially complete. (B) Magnified view of boxed area in A shows that CENP-E is located along and/ or between the interzonal microtubules (boxed). (C) Higher magnification of interzonal microtubules shows that gold particles are primarily located between the microtubule bundles. Bars: (A) 2 μm; (B) 500 nm; (C) 90 nm.
Mentions: To test if detectable CENP-E remains at telophase centromeres, when the functional kinetochores are disassembled, we examined cells in telophase. Fig. 8 A displays a cell in which chromosomes are decondensing and a nuclear lamina has begun to reform around the DNA. No CENP-E was found chromosome associated. Rather, CENP-E was restricted to bundles of antiparallel microtubules in the midzone. For example (Fig. 8 B), in each of five microtubule bundles formed by antiparallel microtubules, CENP-E was found microtubule associated, but only in the electron dense region of overlapping microtubule plus ends (Fig. 8 C).

Bottom Line: Centromere-associated protein E (CENP-E) is a kinesin-related microtubule motor protein that is essential for chromosome congression during mitosis.In congressing chromosomes, CENP-E is preferentially associated with (or accessible at) the stretched, leading kinetochore known to provide the primary power for chromosome movement.Taken together, this evidence strongly supports a model in which CENP-E functions in congression to tether kinetochores to the disassembling microtubule plus ends.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Cell Biology, Ludwig Institute for Cancer Research, School of Medicine, University of California, La Jolla, CA 92093-0660, USA.

ABSTRACT
Centromere-associated protein E (CENP-E) is a kinesin-related microtubule motor protein that is essential for chromosome congression during mitosis. Using immunoelectron microscopy, CENP-E is shown to be an integral component of the kinetochore corona fibers that tether centromeres to the spindle. Immediately upon nuclear envelope fragmentation, an associated plus end motor trafficks cytoplasmic CENP-E toward chromosomes along astral microtubules that enter the nuclear volume. Before or concurrently with initial lateral attachment of spindle microtubules, CENP-E targets to the outermost region of the developing kinetochores. After stable attachment, throughout chromosome congression, at metaphase, and throughout anaphase A, CENP-E is a constituent of the corona fibers, extending at least 50 nm away from the kinetochore outer plate and intertwining with spindle microtubules. In congressing chromosomes, CENP-E is preferentially associated with (or accessible at) the stretched, leading kinetochore known to provide the primary power for chromosome movement. Taken together, this evidence strongly supports a model in which CENP-E functions in congression to tether kinetochores to the disassembling microtubule plus ends.

Show MeSH
Related in: MedlinePlus