Reference Report

Reference
Citation	Kim, M.Y., Bucciarelli, E., Morton, D.G., Williams, B.C., Blake-Hodek, K., Pellacani, C., Von Stetina, J.R., Hu, X., Somma, M.P., Drummond-Barbosa, D., Goldberg, M.L. (2012). Bypassing the Greatwall-Endosulfine Pathway: Plasticity of a Pivotal Cell-Cycle Regulatory Module in Drosophila melanogaster and Caenorhabditis elegans. Genetics 191(4): 1181--1197. (Export to RIS)
FlyBase ID	FBrf0219186
Publication Type	Research paper
PubMed ID	22649080
PubMed Abstract	In vertebrates, mitotic and meiotic M phase is facilitated by the kinase Greatwall (Gwl), which phosphorylates a conserved sequence in the effector Endosulfine (Endos). Phosphorylated Endos inactivates the phosphatase PP2A/B55 to stabilize M-phase-specific phosphorylations added to many proteins by cyclin-dependent kinases (CDKs). We show here that this module functions essentially identically in Drosophila melanogaster and is necessary for proper mitotic and meiotic cell division in a wide variety of tissues. Despite the importance and evolutionary conservation of this pathway between insects and vertebrates, it can be bypassed in at least two situations. First, heterozygosity for loss-of-function mutations of twins, which encodes the Drosophila B55 protein, suppresses the effects of endos or gwl mutations. Several types of cell division occur normally in twins heterozygotes in the complete absence of Endos or the near absence of Gwl. Second, this module is nonessential in the nematode Caenorhaditis elegans. The worm genome does not contain an obvious ortholog of gwl, although it encodes a single Endos protein with a surprisingly well-conserved Gwl target site. Deletion of this site from worm Endos has no obvious effects on cell divisions involved in viability or reproduction under normal laboratory conditions. In contrast to these situations, removal of one copy of twins does not completely bypass the requirement for endos or gwl for Drosophila female fertility, although reducing twins dosage reverses the meiotic maturation defects of hypomorphic gwl mutants. These results have interesting implications for the function and evolution of the mechanisms modulating removal of CDK-directed phosphorylations.
DOI	10.1534/genetics.112.140574
Related Publication(s)
Recent Updates
Description	What does this section display? This section contains items that were added to this record for each release. It currently only tracks new links between this FlyBase report and other FlyBase data classes (e.g. genes, references, stocks) or controlled vocabulary terms (e.g. GO, anatomy terms). What does this section not display? This section does not currently display links that were removed or gene model changes.
Update Feed	Click the icon below to subscribe to this FlyBase record and receive updates automatically through your feed reader.
FB2013_03
FB2013_02
All updates	Click here to see a list of all updates to this record from FB2010_08 and on.
Associated Information
Comments
Associated Files
Other Information
Secondary IDs
Language of Publication	English
Additional Languages of Abstract
Also Published As
Parent Publication
Publication Type	Journal
Abbreviation	Genetics
Title	Genetics
Publication Year	1916-
ISBN/ISSN	0016-6731
Data from Reference
Aberrations (1)
	Df(3L)fz-GF3b
Alleles (18)
	endos⁰⁰⁰⁰³ endos^215-4 endos^EY04709 endos^{S68A.Scer\UAS.P\T} endos^{S68D.Scer\UAS.P\T} endos^{S107A.Scer\UAS.P\T} endos^{S107D.Scer\UAS.P\T} endos^{Scer\UAS.P\T.cKa} gwl¹⁸⁰ gwl⁷¹⁶ gwl¹⁰⁸⁰ gwl²⁷⁹⁰ gwl^Sr18 His2Av^{T:Disc\RFP-mRFP} Scer\GAL4^{nos.UTR.T:Hsim\VP16} tws¹⁹⁶ tws⁴³⁰ tws^j11C8
Constructs (8)
	P{EPgy2} P{GAL4::VP16-nos.UTR} P{His2Av-mRFP1} P{UASp-endos.K} P{UASp-endos.S68A} P{UASp-endos.S68D} P{UASp-endos.S107A} P{UASp-endos.S107D}
Genes (8)
	CG6650 endos gwl His2Av His3 Lam Scer\GAL4 tws
Insertions (1)
	P{EPgy2}endos^EY04709
Natural transposons (1)
	P-element