NDLI: Casein kinase I phosphorylates the Armadillo protein and induces its degradation in Drosophila

Content Provider	PubMed Central
Author	Yanagawa, Shin-ichi Matsuda, Yukihiro Lee, Jong-seo Matsubayashi, Hiroko Sese, Sonoka Kadowaki, Tatsuhiko Ishimoto, Akinori
Copyright Year	2002
Abstract	Casein kinase I (CKI) was recently reported as a positive regulator of Wnt signaling in vertebrates and Caenorhabditis elegans. To elucidate the function of Drosophila CKI in the wingless (Wg) pathway, we have disrupted its function by double-stranded RNA-mediated interference (RNAi). While previous findings were mainly based on CKI overexpression, this is the first convincing loss-of-function analysis of CKI. Surprisingly, CKIα- or CKIε-RNAi markedly elevated the Armadillo (Arm) protein levels in Drosophila Schneider S2R+ cells, without affecting its mRNA levels. Pulse–chase analysis showed that CKI-RNAi stabilizes Arm protein. Moreover, Drosophila embryos injected with CKIα double-stranded RNA showed a naked cuticle phenotype, which is associated with activation of Wg signaling. These results indicate that CKI functions as a negative regulator of Wg/Arm signaling. Overexpression of CKIα induced hyper-phosphorylation of both Arm and Dishevelled in S2R+ cells and, conversely, CKIα-RNAi reduced the amount of hyper-modified forms. His-tagged Arm was phosphorylated by CKIα in vitro on a set of serine and threonine residues that are also phosphorylated by Zeste-white 3. Thus, we propose that CKI phosphorylates Arm and stimulates its degradation.
Related Links	http://dx.doi.org/10.1093/emboj/21.7.1733
Ending Page	1742
Page Count	10
Starting Page	1733
File Format	PDF
ISSN	14602075
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	7
Volume Number	21
Language	English
Publisher	Oxford University Press
Publisher Date	2002-04-01
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia

The C-terminal domain of armadillo binds to hypophosphorylated teashirt to modulate wingless signalling in Drosophila.

Casein kinase 2 associates with and phosphorylates dishevelled.

PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts

The mitogen-activated protein (MAP) kinase ERK induces tRNA synthesis by phosphorylating TFIIIB

Drosophila grim induces apoptosis in mammalian cells.

A casein kinase I motif present in the cytoplasmic domain of members of the tumour necrosis factor ligand family is implicated in 'reverse signalling'.

Akt phosphorylates acinus and inhibits its proteolytic cleavage, preventing chromatin condensation

Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signaling.

Casein kinase I phosphorylates the Armadillo protein and induces its degradation in Drosophila

Similar Documents

Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia

The C-terminal domain of armadillo binds to hypophosphorylated teashirt to modulate wingless signalling in Drosophila.

Casein kinase 2 associates with and phosphorylates dishevelled.

PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts

The mitogen-activated protein (MAP) kinase ERK induces tRNA synthesis by phosphorylating TFIIIB

Drosophila grim induces apoptosis in mammalian cells.

A casein kinase I motif present in the cytoplasmic domain of members of the tumour necrosis factor ligand family is implicated in 'reverse signalling'.

Akt phosphorylates acinus and inhibits its proteolytic cleavage, preventing chromatin condensation

Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signaling.

Casein kinase I phosphorylates the Armadillo protein and induces its degradation in Drosophila