Unknown

Dataset Information

0

The Drosophila kinesin-like protein KLP67A is essential for mitotic and male meiotic spindle assembly.


ABSTRACT: We have performed a mutational analysis together with RNA interference to determine the role of the kinesin-like protein KLP67A in Drosophila cell division. During both mitosis and male meiosis, Klp67A mutations cause an increase in MT length and disrupt discrete aspects of spindle assembly, as well as cytokinesis. Mutant cells exhibit greatly enlarged metaphase spindle as a result of excessive MT polymerization. The analysis of both living and fixed cells also shows perturbations in centrosome separation, chromosome segregation, and central spindle assembly. These data demonstrate that the MT plus end-directed motor KLP67A is essential for spindle assembly during mitosis and male meiosis and suggest that the regulation of MT plus-end polymerization is a key determinant of spindle architecture throughout cell division.

SUBMITTER: Gandhi R 

PROVIDER: S-EPMC307533 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

The Drosophila kinesin-like protein KLP67A is essential for mitotic and male meiotic spindle assembly.

Gandhi Rita R   Bonaccorsi Silvia S   Wentworth Diana D   Doxsey Stephen S   Gatti Maurizio M   Pereira Andrea A  

Molecular biology of the cell 20030917 1


We have performed a mutational analysis together with RNA interference to determine the role of the kinesin-like protein KLP67A in Drosophila cell division. During both mitosis and male meiosis, Klp67A mutations cause an increase in MT length and disrupt discrete aspects of spindle assembly, as well as cytokinesis. Mutant cells exhibit greatly enlarged metaphase spindle as a result of excessive MT polymerization. The analysis of both living and fixed cells also shows perturbations in centrosome  ...[more]

Similar Datasets

| S-EPMC4042853 | biostudies-other
| S-EPMC7295595 | biostudies-literature
| S-EPMC11001723 | biostudies-literature
| S-EPMC2132492 | biostudies-literature
| S-EPMC2289520 | biostudies-other
| S-EPMC5797964 | biostudies-literature
| S-EPMC1237074 | biostudies-literature
| S-EPMC4034379 | biostudies-literature
| S-EPMC4180425 | biostudies-literature
| S-EPMC2837481 | biostudies-literature