In vitro and in vivo analysis of microtubule-destabilizing kinesins.
Cellular microtubules are rigid in comparison to other cytoskeletal elements (1,2). To facilitate cytoplasmic remodeling and timely responses to cell signaling events, microtubules depolymerize and repolymerize rapidly at their ends (3). These dynamic properties are critically important for many cellular functions, such as spindle assembly, the capture and segregation of chromosomes during cell division and cell motility. Microtubule dynamics are spatially and temporally controlled in the cell by accessory proteins. Molecular motor proteins of the kinesin superfamily that act to destabilize microtubules play important roles in this regulation (4).
Stumpff
Jason
J
Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA, USA.
Cooper
Jeremy
J
Domnitz
Sarah
S
Moore
Ayana T
AT
Rankin
Kathleen E
KE
Wagenbach
Mike
M
Wordeman
Linda
L
D000818:Animals; D001665:Binding Sites; D001671:Biochemistry / Q000379:methods*; D016466:CHO Cells; D002455:Cell Division; D002465:Cell Movement; D006224:Cricetinae; D003412:Cricetulus; D003599:Cytoskeleton / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D066298:In Vitro Techniques; D016547:Kinesins / Q000737:chemistry / Q000502:physiology*; D008870:Microtubules / Q000737:chemistry* / Q000378:metabolism; D020409:Molecular Motor Proteins / Q000378:metabolism; D015398:Signal Transduction; D014404:Tubulin / Q000737:chemistry
D020409:Molecular Motor Proteins; D014404:Tubulin; D016547:Kinesins