Heterodimerization of the Two Motor Subunits of the Heterotrimeric Kinesin, KRP85/95

Rashid, Dana; Wedaman, Karen P.; Scholey, Jonathan M.

doi:10.1006/jmbi.1995.0484

Cited by 60 publications

(87 citation statements)

References 12 publications

(24 reference statements)

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“…2D, like the full-length Kif3C protein (14,24), the truncated Kif3C protein also specifically associates with Kif3A but not Kif3B. It was suggested previously that opposing charge interactions within the stalk domains of the Kif3 family are important for generating heterodimers (17). This region, however, is deleted in the Kif3C typeI (Ϫ/Ϫ) mice.…”

Section: Methodsmentioning

confidence: 90%

Functional Analysis of Mouse Kinesin Motor Kif3C

Yang

Roberts

Goldstein

2001

Molecular and Cellular Biology

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Members of the kinesin II family are thought to play essential roles in many types of intracellular transport. One distinguishing feature of kinesin II is that it generally contains two different motor subunits from the Kif3 family. Three Kif3 family members (Kif3A, Kif3B, and Kif3C) have been identified and characterized in mice. Intracellular localization and biochemical studies previously suggested that Kif3C is an anterograde motor involved in anterograde axonal transport. To understand the in vivo function of the Kif3C gene, we used homologous recombination in embryonic stem cells to construct two different knockout mouse strains for the Kif3C gene. Both homozygous Kif3C mutants are viable, reproduce normally, and apparently develop normally. These results suggest that Kif3C is dispensable for normal neural development and behavior in the mouse.

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Section: Methodsmentioning

confidence: 90%

Functional Analysis of Mouse Kinesin Motor Kif3C

Yang

Roberts

Goldstein

2001

Molecular and Cellular Biology

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“…Two forms of kinesin-II, which share a characteristic signature sequence (EDPKDALLRF/Y) in their neck domains, are thought to function as motors that drive anterograde IFT, namely heterotrimeric kinesin-II (also known as FLA-10-kinesin-II or KIF3A/3B/KAP3) and homodimeric kinesin-II (also known as Osm-3-kinesin or KIF 17) ( Figure 2b). Heterotrimeric kinesin-II was first purified from sea urchin embryonic cytosol via MT-affinity with the aid of pan-kinesin antibodies (Cole et al 1992(Cole et al , 1993Rashid et al 1995;Wedaman et al 1996), and it has subsequently been isolated from organisms ranging from algae to mammals (Yamazaki et al 1996, Cole et al 1998, Signor et al 1999b, Scholey 1996, Marszalek & Goldstein 2000. Heterotrimeric kinesin-II holoenzymes contain two distinct motor subunits whose heterodimerization is directed by complementary charge interactions in a segment of the 35-nm long coiled-coil rod (De Marco et al 2001).…”

Section: The Protein Machinery Of Iftmentioning

confidence: 99%

Intraflagellar Transport

Scholey

2003

Annu. Rev. Cell Dev. Biol.

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380

374

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s Abstract It has been a decade since a novel form of microtubule (MT)-based motility, i.e., intraflagellar transport (IFT), was discovered in Chlamydomonas flagella. Subsequent research has supported the hypothesis that IFT is required for the assembly and maintenance of all cilia and flagella and that its underlying mechanism involves the transport of nonmembrane-bound macromolecular protein complexes (IFT particles) along axonemal MTs beneath the ciliary membrane. IFT requires the action of the anterograde kinesin-II motors and the retrograde IFT-dynein motors to transport IFT particles in opposite directions along the MT polymer lattice from the basal body to the tip of the axoneme and back again. A rich diversity of biological processes has been shown to depend upon IFT, including flagellar length control, cell swimming, mating and feeding, photoreception, animal development, sensory perception, chemosensory behavior, and lifespan control. These processes reflect the varied roles of cilia and flagella in motility and sensory signaling.

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“…Using a biochemical approach, they purified an active heterotrimeric microtubule motor complex (KRP85/95) from Strongylocentrotus purpuratus that contains two different kinesin-like motor subunits, SpKRP85 and SpKRP95, and a 115-kDa associated protein. The novel feature of KRP85/95 is the ability of its two kinesinlike subunits to heterodimerize, possibly through their coiled-coil stalk domains (121). This may be a general principle, since related KLPs have been identified in mouse (66,122,123), Drosophila (124), Chlamydomonas (125), and Caenorhabditis (44,124), suggesting that these KLPs are members of a new kinesin family (4, 84).…”

Section: Gaps In Our Understandingmentioning

confidence: 99%

Going mobile: microtubule motors and chromosome segregation.

Barton

Goldstein²

1996

Proc. Natl. Acad. Sci. U.S.A.

156

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Proper chromosome segregation in eukaryotes depends upon the mitotic and meiotic spindles, which assemble at the time of cell division and then disassemble upon its completion. These spindles are composed in large part of microtubules, which either generate force by controlled polymerization and depolymerization or transduce force generated by molecular microtubule motors. In this review, we discuss recent insights into chromosome segregation mechanisms gained from the analyses of force generation during meiosis and mitosis. These analyses have demonstrated that members of the kinesin superfamily and

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Heterodimerization of the Two Motor Subunits of the Heterotrimeric Kinesin, KRP85/95

Cited by 60 publications

References 12 publications

Functional Analysis of Mouse Kinesin Motor Kif3C

Functional Analysis of Mouse Kinesin Motor Kif3C

Intraflagellar Transport

Going mobile: microtubule motors and chromosome segregation.

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