spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Armstrong, C. G.
Right arrow Articles by Cohen, P. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Armstrong, C. G.
Right arrow Articles by Cohen, P. T.

Journal of Cell Science, Vol 108, Issue 11 3367-3375, Copyright © 1995 by Company of Biologists

JOURNAL ARTICLES

Drosophila PPY, a novel male specific protein serine/threonine phosphatase localised in somatic cells of the testis

CG Armstrong, DJ Mann, N Berndt and PT Cohen
Department of Biochemistry, University, Dundee, Scotland, UK.

Drosophila protein phosphatase Y (PPY) displays 64% amino acid identity to protein serine/threonine phosphatase 1 (PP1) and 39% to protein phosphatase 2A (PP2A). Here we show by expression of cDNA in bacteria, that PPY is a protein serine phosphatase and that its biochemical properties are distinct from PP1 in both substrate specificity and regulation by the thermostable inhibitory proteins inhibitor 1 and inhibitor 2. We also demonstrate that PPY is a novel testis specific protein phosphatase by analysis of both mRNA and protein distribution. More precise immunolocalisation within the testis, using affinity purified anti-PPY protein and anti-PPY peptide antibodies, shows that PPY is present in somatic cyst cells, which encase the germ cells. The predominant location of PPY is in the nuclei of both head and tail cyst cells throughout the length of the testis except for the apical tip. The distribution of PPY, coupled with its unique biochemical properties, suggests that PPY may be required to prevent cyst cell division, increase transcription for provision of nutrients to the germ cells and/or provide a signal for spermatocyte differentiation.


This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
A. Jung, M. Hollmann, and M. A. Schafer
The fatty acid elongase NOA is necessary for viability and has a somatic role in Drosophila sperm development
J. Cell Sci., August 15, 2007; 120(16): 2924 - 2934.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
M. L. Sohaskey and J. E. Ferrell Jr.
Distinct, Constitutively Active MAPK Phosphatases Function in Xenopus Oocytes: Implications for p42 MAPK Regulation In Vivo
Mol. Biol. Cell, November 1, 1999; 10(11): 3729 - 3743.
[Abstract] [Full Text]

Home page
 J. Cell Sci.Home page
N. Helps, N. Brewis, K Lineruth, T Davis, K Kaiser, and P. Cohen
Protein phosphatase 4 is an essential enzyme required for organisation of microtubules at centrosomes in Drosophila embryos
J. Cell Sci., January 5, 1998; 111(10): 1331 - 1340.
[Abstract] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. M. Travis, H. A. Berger, and M. J. Welsh
Protein phosphatase 2C dephosphorylates and inactivates cystic fibrosis transmembrane conductance regulator
PNAS, September 30, 1997; 94(20): 11055 - 11060.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
H. Snaith, C. Armstrong, Y Guo, K Kaiser, and P. Cohen
Deficiency of protein phosphatase 2A uncouples the nuclear and centrosome cycles and prevents attachment of microtubules to the kinetochore in Drosophila microtubule star (mts) embryos
J. Cell Sci., January 12, 1996; 109(13): 3001 - 3012.
[Abstract] [PDF]


© The Company of Biologists Ltd 1995