KAR3, a kinesin-related gene required for yeast nuclear fusion

 KAR3, a kinesin-related gene required for yeast nuclear fusion},
  author={Pamela B Meluh and Mark D Rose},

Mechanistic Analysis of the Saccharomyces cerevisiae Kinesin Kar3*

The results indicate that the extended α-helical domain NH2-terminal to the catalytic core provides the structural transitions in response to the ATPase cycle that are critical for motility and that dimerization is not specifically required.

Kid, a novel kinesin‐like DNA binding protein, is localized to chromosomes and the mitotic spindle.

Indirect immunofluorescence studies show that Kid colocalizes with mitotic chromosomes and that it is enriched in the kinetochore at anaphase, suggesting that Kid might play a role in regulating the chromosomal movement along microtubules during mitosis.

Fission yeast pkl1 is a kinesin-related protein involved in mitotic spindle function.

It is proposed that pkl1 functions as a microtubules-dependent motor that is involved in microtubule organization in the mitotic spindle.

MHP1, an essential gene in Saccharomyces cerevisiae required for microtubule function

Results suggest that MHP1 is essential for the formation and/or stabilization of microtubules.

The Kar3p kinesin-related protein forms a novel heterodimeric structure with its associated protein Cik1p.

Mapping of the interaction domains of the two proteins by two-hybrid analyses indicates that Kar3p and Cik1p associate in a highly specific manner along the lengths of their respective coiled-coil domains, demonstrating that the Kar3-Cik1 complex has a novel heterodimeric structure not observed previously for kinesin complexes.

Localization of the Kar3 kinesin heavy chain-related protein requires the Cik1 interacting protein

Analysis by both the two-hybrid system and co- immunoprecipitation experiments indicates that Cik1p and kar3p interact, suggesting that they are part of the same protein complex, which can determine the localization of motor activity and thereby affect the functional specificity of the motor complex.

The Chlamydomonas FLA10 gene encodes a novel kinesin-homologous protein

Results indicate that KHP1 is the gene product of FLA10 and suggest a novel role for this kinesin-related protein in flagellar assembly and maintenance.

Characterization of a minus end-directed kinesin-like motor protein from cultured mammalian cells

Using the CHO2 monoclonal antibody raised against CHO spindles, a 66-kD protein located at the interphase centrosome and mitotic spindle was identified and revealed the presence of 340-amino acid residues in the COOH terminus, which is homologous to the motor domain conserved among other members of the kinesin superfamily.

KAR5 Encodes a Novel Pheromone-inducible Protein Required for Homotypic Nuclear Fusion

It is proposed that Kar5p is required for the completion of nuclear membrane fusion and may play a role in the organization of the membrane fusion complex.



Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein

The data imply that the carboxyl-terminal domain containing the 18-amino acid repeats constitutes the microtubule binding site in MAP2, a prominent large-sized component of purified brain microtubules that bears antigenic determinants found in association with the neurofibrillary tangles of Alzheimer's disease.

Diverse effects of beta-tubulin mutations on microtubule formation and function

Using five new cold-sensitive mutations in TUB2, the sole gene encoding beta- tubulin in the yeast Saccharomyces cerevisiae, it is demonstrated that cytoplasmic microtubules are necessary fornuclear migration during the mitotic cell cycle and for nuclear migration and fusion during conjugation; only those mutants that possess cy toplasmo microtubule arrays are able to perform these functions.

MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties

Characteristics suggest that MAP 1C may be a cytoplasmic analogue of axonemal dynein, and is enriched in microtubules prepared in the absence of nucleotide.

Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindle

The identification and isolation of a kinesin-like protein from the cytoplasm of sea urchin eggs is described and proposed that it may be a mechanochemical factor for some form of motility associated with the mitotic spindle.