Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains

Ishikawa, HO, Takeuchi H, Haltiwanger RS, Irvine KD.  2008.  

Journal:

Science

Volume Number:

321

Pages:

401-4

Abstract:

The atypical cadherin Fat acts as a receptor for a signaling pathway that regulates growth, gene expression, and planar cell polarity. Genetic studies in Drosophila identified the four-jointed gene as a regulator of Fat signaling. We show that four-jointed encodes a protein kinase that phosphorylates serine or threonine residues within extracellular cadherin domains of Fat and its transmembrane ligand, Dachsous. Four-jointed functions in the Golgi and is the first molecularly defined kinase that phosphorylates protein domains destined to be extracellular. An acidic sequence motif (Asp-Asn-Glu) within Four-jointed was essential for its kinase activity in vitro and for its biological activity in vivo. Our results indicate that Four-jointed regulates Fat signaling by phosphorylating cadherin domains of Fat and Dachsous as they transit through the Golgi.

Related External URL:

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=18635802
Citation:
Ishikawa, HO, Takeuchi H, Haltiwanger RS, Irvine KD.  2008.  Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains. Science. 321:401-4.