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PMID: 9701548 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Assembly and dynamics of an anastral:astral spindle: the meiosis II spindle of Drosophila oocytes.

Journal of cell science ·Vol. 111 ( Pt 17) ·1998-09-00 ·Pages 2487-95

Endow SA, Komma DJ

Abstract

The meiosis II spindle of Drosophila oocytes is distinctive in structure, consisting of two tandem spindles with anastral distal poles and an aster-associated spindle pole body between the central poles. Assembly of the anastral:astral meiosis II spindle occurs by reorganization of the meiosis I spindle, without breakdown of the meiosis I spindle. The unusual disk- or ring-shaped central spindle pole body forms de novo in the center of the elongated meiosis I spindle, followed by formation of the central spindle poles. gamma-Tubulin transiently localizes to the central spindle pole body, implying that the body acts as a microtubule nucleating center for assembly of the central poles. Localization of gamma-tubulin to the meiosis II spindle is dependent on the microtubule motor protein, Nonclaret disjunctional (Ncd). Absence of Ncd results in loss of gamma-tubulin localization to the spindle and destabilization of microtubules in the central region of the spindle. Assembly of the anastral:astral meiosis II spindle probably involves rapid reassortment of microtubule plus and minus ends in the center of the meiosis I spindle - this can be accounted for by a model that also accounts for the loss of gamma-tubulin localization to the spindle and destabilization of microtubules in the absence of Ncd.

MeSH Terms
Adenosine Triphosphatases Animals Drosophila/cytology,embryology Drosophila Proteins Genetic Complementation Test Immunohistochemistry Kinesins/genetics Meiosis/physiology Microtubules/metabolism Mutation Oocytes/cytology Ovum/cytology Spindle Apparatus/metabolism,physiology Tubulin/analysis,genetics,metabolism
Chemicals
Drosophila Proteins Tubulin ncd protein, Drosophila Adenosine Triphosphatases Kinesins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Endow S A
Department of Microbiology, Duke University Medical Center, Durham, NC 27710, USA. endow@galactose.mc.duke.edu
Komma D J
Article Info
Journal
Journal of cell science
Abbr.
J Cell Sci
ISSN
0021-9533
Published
1998-09-00
Pages
2487-95
Language
English
Region
England
NLM ID
0052457
Subset
IM
Grants
NIGMS NIH HHS · R01 GM046225 · United States
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