Abstract
The dynamic behavior of homotetrameric kinesin-5 during mitosis is poorly understood. Kinesin-5 may function only by binding, cross-linking, and sliding adjacent spindle microtubules (MTs), or, alternatively, it may bind to a stable " spindle matrix " to generate mitotic movements. We created transgenic Drosophila melanogaster expressing fluorescent kinesin-5, KLP61F-GFP, in a klp61f mutant background, where it rescues mitosis and viability. KLP61F-GFP localizes to interpolar MT bundles, half spindles, and asters, and is enriched around spindle poles. In fluorescence recovery after photobleaching experiments, KLP61F-GFP displays dynamic mobility similar to tubulin, which is inconsistent with a substantial static pool of kinesin-5. The data conform to a reaction - diffusion model in which most KLP61F is bound to spindle MTs, with the remainder diffusing freely. KLP61F appears to transiently bind MTs, moving short distances along them before detaching. Thus, kinesin-5 motors can function by cross-linking and sliding adjacent spindle MTs without the need for a static spindle matrix.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 429-436 |
| Number of pages | 8 |
| Journal | Journal of Cell Biology |
| Volume | 182 |
| Issue number | 3 |
| DOIs | |
| State | Published - Aug 11 2008 |
Fingerprint
ASJC Scopus subject areas
- Cell Biology
Cite this
Dynamic partitioning of mitotic kinesin-5 cross-linkers between microtubule-bound and freely diffusing states. / Cheerambathur, Dhanya K.; Brust-Mascher, Ingrid; Civelekoglu-Scholey, Gul; Scholey, Jonathan M.
In: Journal of Cell Biology, Vol. 182, No. 3, 11.08.2008, p. 429-436.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dynamic partitioning of mitotic kinesin-5 cross-linkers between microtubule-bound and freely diffusing states
AU - Cheerambathur, Dhanya K.
AU - Brust-Mascher, Ingrid
AU - Civelekoglu-Scholey, Gul
AU - Scholey, Jonathan M.
PY - 2008/8/11
Y1 - 2008/8/11
N2 - The dynamic behavior of homotetrameric kinesin-5 during mitosis is poorly understood. Kinesin-5 may function only by binding, cross-linking, and sliding adjacent spindle microtubules (MTs), or, alternatively, it may bind to a stable " spindle matrix " to generate mitotic movements. We created transgenic Drosophila melanogaster expressing fluorescent kinesin-5, KLP61F-GFP, in a klp61f mutant background, where it rescues mitosis and viability. KLP61F-GFP localizes to interpolar MT bundles, half spindles, and asters, and is enriched around spindle poles. In fluorescence recovery after photobleaching experiments, KLP61F-GFP displays dynamic mobility similar to tubulin, which is inconsistent with a substantial static pool of kinesin-5. The data conform to a reaction - diffusion model in which most KLP61F is bound to spindle MTs, with the remainder diffusing freely. KLP61F appears to transiently bind MTs, moving short distances along them before detaching. Thus, kinesin-5 motors can function by cross-linking and sliding adjacent spindle MTs without the need for a static spindle matrix.
AB - The dynamic behavior of homotetrameric kinesin-5 during mitosis is poorly understood. Kinesin-5 may function only by binding, cross-linking, and sliding adjacent spindle microtubules (MTs), or, alternatively, it may bind to a stable " spindle matrix " to generate mitotic movements. We created transgenic Drosophila melanogaster expressing fluorescent kinesin-5, KLP61F-GFP, in a klp61f mutant background, where it rescues mitosis and viability. KLP61F-GFP localizes to interpolar MT bundles, half spindles, and asters, and is enriched around spindle poles. In fluorescence recovery after photobleaching experiments, KLP61F-GFP displays dynamic mobility similar to tubulin, which is inconsistent with a substantial static pool of kinesin-5. The data conform to a reaction - diffusion model in which most KLP61F is bound to spindle MTs, with the remainder diffusing freely. KLP61F appears to transiently bind MTs, moving short distances along them before detaching. Thus, kinesin-5 motors can function by cross-linking and sliding adjacent spindle MTs without the need for a static spindle matrix.
UR - http://www.scopus.com/inward/record.url?scp=49749121135&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=49749121135&partnerID=8YFLogxK
U2 - 10.1083/jcb.200804100
DO - 10.1083/jcb.200804100
M3 - Article
C2 - 18678711
AN - SCOPUS:49749121135
VL - 182
SP - 429
EP - 436
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 3
ER -