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PMID: 9570751 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Protein phosphatase 4 is an essential enzyme required for organisation of microtubules at centrosomes in Drosophila embryos.

Journal of cell science ·Vol. 111 ( Pt 10) ·1998-05-00 ·Pages 1331-40

Helps NR, Brewis ND, Lineruth K, Davis T, Kaiser K, Cohen PT

Abstract

The protein serine/threonine phosphatase 4 (PP4), which localises to centrosomes/spindle pole bodies in human cells, is shown to exhibit a similar localisation in Drosophila cells and embryos and possess a highly conserved (91% identical) amino acid sequence from humans to invertebrates. A homozygous Drosophila melanogaster strain mutant in the PP4 gene at 19C1-2 has been produced using P element mutagenesis. This strain, termed centrosomes minus microtubules (cmm), has reduced amounts of PP4 mRNA, approximately 25% of normal PP4 protein in early embryos and exhibits a semi-lethal phenotype with only 10% viability in certain conditions. Reversion mutagenesis shows that the phenotype is due to the presence of the P element in the PP4 mRNA. In early cmm embryos, nuclear divisions become asynchronous and large regions containing centrosomes with no well defined radiating microtubules are visible. In such areas, most nuclei arrest during mitosis with condensed DNA, and mitotic spindle microtubules are either absent, or aberrant and unconnected to the centrosome. A reduction in the staining of gamma-tubulin at centrosomes in cmm embryos suggests a conformational change or relocation of this protein, which is known to be essential for initiation of microtubule growth. These findings indicate that PP4 is required for nucleation, growth and/or stabilisation of microtubules at centrosomes/spindle pole bodies.

MeSH Terms
Animals Centrosome/metabolism Conserved Sequence DNA, Complementary Drosophila/enzymology,genetics,growth & development Fluorescent Antibody Technique Genes, Insect Homozygote Mammals Microtubules/metabolism Mitosis/genetics Molecular Sequence Data Mutagenesis, Insertional/physiology Phenotype Phosphorylation Protein Serine-Threonine Kinases/analysis,genetics,metabolism RNA, Messenger/analysis Sequence Homology, Amino Acid Spindle Apparatus/metabolism
Chemicals
DNA, Complementary RNA, Messenger Protein Serine-Threonine Kinases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Helps N R
Medical Research Council Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland, UK.
Brewis N D
Lineruth K
Davis T
Kaiser K
Cohen P T
Article Info
Journal
Journal of cell science
Abbr.
J Cell Sci
ISSN
0021-9533
Published
1998-05-00
Pages
1331-40
Language
English
Region
England
NLM ID
0052457
Subset
IM
Databases
GENBANK
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