Europe PMC

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our privacy notice and cookie policy.

Proteolysis of the Hedgehog signaling effector Cubitus interruptus requires phosphorylation by Glycogen Synthase Kinase 3 and Casein Kinase 1.

Author information

Affiliations

  • 1. Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
      Authors
    • Price MA 1
    (1 author)

Cell, 01 Mar 2002, 108(6):823-835
https://doi.org/10.1016/s0092-8674(02)00664-5 PMID: 11955435 

Abstract 

The secreted signaling molecule Hedgehog regulates gene expression in target cells in part by preventing proteolysis of the full-length Cubitus interruptus (Ci-155) transcriptional activator to the Ci-75 repressor form. Ci-155 proteolysis depends on phosphorylation at three sites by Protein Kinase A (PKA). We show that these phosphoserines prime further phosphorylation at adjacent Glycogen Synthase Kinase 3 (GSK3) and Casein Kinase I (CK1) sites. Alteration of the GSK3 or CK1 sites prevents Ci-155 proteolysis and activates Ci in the absence of Hedgehog. Ci-155 proteolysis is also inhibited if cells lack activity of the Drosophila GSK3, Shaggy, previously implicated in Wingless signaling. Conversely, Ci-155 levels are reduced in Hedgehog-responding cells by overexpression of PKA and the Drosophila CK1, Double-time, a regulator of circadian rhythms.

Full text links 

Read article at publisher's site: https://doi.org/10.1016/s0092-8674(02)00664-5

Read article for free, from open access legal sources, via Unpaywall: http://www.cell.com/article/S0092867402006645/pdfUnpaywall

References 

Articles referenced by this article (54)

Show 10 more references (10 of 54)

Citations & impact 

Impact metrics

252
Citations
Jump to Citations
12
Data citations
Jump to Data

Citations of article over time

Alternative metrics

Altmetric item for https://www.altmetric.com/details/102515979
Altmetric
Discover the attention surrounding your research
https://www.altmetric.com/details/102515979

Smart citations by scite.ai
Smart citations by scite.ai include citation statements extracted from the full text of the citing article. The number of the statements may be higher than the number of citations provided by EuropePMC if one paper cites another multiple times or lower if scite has not yet processed some of the citing articles.
Explore citation contexts and check if this article has been supported or disputed.
https://scite.ai/reports/10.1016/s0092-8674(02)00664-5

Supporting
Mentioning
Contrasting
9
312
1

Article citations

Go to all (252) article citations

Other citations

Data 

Similar Articles 

To arrive at the top five similar articles we use a word-weighted algorithm to compare words from the Title and Abstract of each citation.

Funding 

Funders who supported this work.

NIGMS NIH HHS (1)