A new look at the microtubule binding patterns of dimeric kinesins11Edited by W. Baumeister

Hoenger, Andreas; Thormählen, Manfred; Díaz-Avalos, Rubén; Doerhoefer, Monika; Goldie, Kenneth N.; Müller, Jens; Mandelkow, Eckhard

doi:10.1006/jmbi.2000.3627

Cited by 104 publications

(144 citation statements)

References 67 publications

(158 reference statements)

Supporting

Mentioning

123

Contrasting

Order By: Relevance

“…As expected from previous results, monomeric kinesin motor heads bind to sheets in a regular B-lattice type pattern (Amos and Klug, 1974) revealing a strong 8 nm periodicity. Dimeric kinesins, however, revealed a significantly less ordered surface caused by their binding characteristics as predicted by Hoenger et al (2000). Interestingly, the sheet surface corresponding to the microtubule inner side revealed surprisingly strong differences between the ␣-and ␤-tubulin units, similar to earlier observations made on negatively stained samples (Hoenger et al, 1995;Hoenger and Milligan, 1997).…”

Section: Introductionsupporting

confidence: 83%

“…Taken together, Figures 3A-C and Figures 3D-F reveal a good picture of the surface topography of the outer and inner surface of kinesin-decorated tubulin sheets, which compares well with existing 3-D data. The topographies of the outer surfaces show comparable features to 3-D reconstructions of frozen hydrated kinesin-microtubule complexes (e. g. see Hoenger et al, 1998Hoenger et al, , 2000 and even allow an indirect polarity determination. Judging by the accumulation of metal (which appears bright) the kinesin head appears clearly higher and slightSurface Topography of Kinesin-Microtubule Complexes 1005 Two shadowing directions at different azimuth angles are shown (circled arrows).…”

Section: Surface Shadowing Of Tubulin Sheets Decorated With Monomericmentioning

confidence: 67%

“…The availability of atomic resolution X-ray structures of monomeric and dimeric kinesin Sack et al, 1997;Kozielski et al, 1997) and ncd (Sablin et al, , 1998 in combination with the near-atomic resolution EM-structure of zinc-induced tubulin sheets (Nogales et al, 1998) now provide detailed pictures of the microtubule structure (Nogales et al, 1999) and of the kinesin-tubulin complex (Hoenger et al, 2000;Kikkawa et al, 2000). There is now a general consensus on the tubulin interaction and binding geometry of monomeric kinesin and ncd (Hirose et al, 1995;Hoenger et al, 1995;Kikkawa et al, 1995;Arnal et al 1996;Hoenger and Milligan, 1997).…”

Section: Introductionmentioning

confidence: 99%

“…Recent cryo-EM and scanning transmission electron microscopy (STEM)-based mass determinations (Müller et al, 1992) demonstrated the complexity of dimeric kinesin interaction with microtubules Hoenger et al 2000). While there is agreement on the arrangement of dimeric ncd (a retrograde kinesin-like motor) on the microtubule surface (Sosa et al, 1997;Hirose et al, 1998), divergent interpretations have been given for the interaction of dimeric kinesin with microtubules (Arnal et al, 1996;Hirose et al, 1996Hirose et al, , 1999Hoenger et al, 1998Hoenger et al, , 2000. This situation has prompted us to study motor-microtubule complexes using complementary structural methods.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Surface Topography of Microtubule Walls Decorated with Monomeric and Dimeric Kinesin Constructs

Hoenger

Doerhoefer²,

Woehlke³

et al. 2000

Biological Chemistry

Self Cite

View full text Add to dashboard Cite

The surface topography of opened-up microtubule walls (sheets) decorated with monomeric and dimeric kinesin motor domains was investigated by freezedrying and unidirectional metal shadowing. Electron microscopy of surface-shadowed specimens produces images with a high signal/noise ratio, which enable a direct observation of surface features below 2 nm detail. Here we investigate the inner and outer surface of microtubules and tubulin sheets with and without decoration by kinesin motor domains. Tubulin sheets are flattened walls of microtubules, keeping lateral protofilament contacts intact. Surface shadowing reveals the following features: (i) when the microtubule outside is exposed the surface relief is dominated by the bound motor domains. Monomeric motor constructs generate a strong 8 nm periodicity, corresponding to the binding of one motor domain per ␣-␤-tubulin heterodimer. This surface periodicity largely disappears when dimeric kinesin motor domains are used for decoration, even though it is still visible in negatively stained or frozen hydrated specimens. This could be explained by disorder in the binding of the second (loosely tethered) kinesin head, and/or disorder in the coiled-coil tail. (ii) Both surfaces of undecorated sheets or microtubules, as well as the inner surface of decorated sheets, reveal a strong 4 nm repeat (due to the periodicity of tubulin monomers) and a weak 8 nm repeat (due to slight differences between ␣-and ␤-tubulin). The differences between ␣-and ␤-tubulin on the inner surface are stronger than expected from cryo-electron microscopy of unstained microtubules, indicating the existence of tubulin subdomain-specific surface properties that reflect the surface corrugation and hence metal deposition during evaporation. The 16 nm periodicity visible in some negatively stained specimens (caused by the pairing of cooperatively bound kinesin dimers) is not detected by surface shadowing.

show abstract

Section: Introductionsupporting

confidence: 83%

Section: Surface Shadowing Of Tubulin Sheets Decorated With Monomericmentioning

confidence: 67%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Surface Topography of Microtubule Walls Decorated with Monomeric and Dimeric Kinesin Constructs

Hoenger

Doerhoefer²,

Woehlke³

et al. 2000

Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…However, weak interactions between motors might be templated by the MT lattice. Such unexpected core motor domain dimerizations have been seen before, particularly (and inexplicably) with proteins isolated from cold-blooded animals such as Drosophila and squid (31). Alternatively, as is thought to occur with mammalian kinesin-13 family member, MCAK, one motor may crosslink the protofilament to the MT from either side.…”

Section: Kinesin-13: Bracelets Of Tubulinmentioning

confidence: 75%

Rings, bracelets, sleeves, and chevrons: new structures of kinetochore proteins

Davis

Wordeman

2007

Trends in Cell Biology

View full text Add to dashboard Cite

Electron microscopy has recently revealed striking structural orderliness in kinetochore proteins and protein complexes that associate with microtubules. In addition to their astonishing appearance and intrinsic beauty, the structures are functionally informative. The Dam1 and Ndc80 complexes bind to the microtubule lattice as rings and chevrons, respectively. These structures give insight into how the kinetochore couples to dynamic microtubules, a process critical to the accurate segregation of chromosomes. HURP and kinesin-13 arrange tubulin into sleeves and bracelets surrounding the microtubule lattice. These structures may reflect the ability of these proteins to modulate microtubule dynamics by interacting with specialized tubulin configurations. In this review, we compare and contrast the structure of these proteins and their interactions with microtubules to illustrate how they may attach to and modulate the dynamics of microtubules.

show abstract

A Missense Mutation in the Coiled-Coil Domain of the KIF5A Gene and Late-Onset Hereditary Spastic Paraplegia

Giudice¹,

Neri²,

Falco³

et al. 2006

Arch Neurol

View full text Add to dashboard Cite

Background: To our knowledge, up to now, only 2 mutations in the KIF5A gene, a member of the kinesin superfamily, have been identified as the molecular cause of early-onset autosomal dominant hereditary spastic paraparesis (ADHSP). Objective: To assess the genetic defect in a family with late-onset ADHSP. Patients and Methods: Only the proband agreed to undergo complete neurological testing and mutational analysis. The proband was screened for mutations in the spastin, atlastin, NIPA1, and KIF5A genes, either by denaturing high-performance liquid chromatography or sequence analysis. Results: The history of the family was consistent with ADHSP characterized by late onset of the disease. Mutational analysis results were negative for the spastin, atlastin, and NIPA1 genes but identified a missense mutation (c.1082CϾT) in the coiled-coil coding region of the KIF5A gene. Conclusions: This finding enlarges the phenotypic spectrum of ADHSP linked to KIF5A and enhances the role of that gene in the epidemiology of this disease. We propose that the KIF5A gene should be routinely analyzed in patients with hereditary spastic paraplegia negative for spastin and atlastin mutations.

show abstract

A new look at the microtubule binding patterns of dimeric kinesins11Edited by W. Baumeister

Cited by 104 publications

References 67 publications

Surface Topography of Microtubule Walls Decorated with Monomeric and Dimeric Kinesin Constructs

Surface Topography of Microtubule Walls Decorated with Monomeric and Dimeric Kinesin Constructs

Rings, bracelets, sleeves, and chevrons: new structures of kinetochore proteins

A Missense Mutation in the Coiled-Coil Domain of the KIF5A Gene and Late-Onset Hereditary Spastic Paraplegia

Contact Info

Product

Resources

About