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1 Biologie cellulaire des homéoprotéines, CNRS UMR8542 Ecole Normale Supérieure 46 rue d’Ulm F-75005 Paris, France
2 INSERM EMI 0104 DBMS CEA, 17 rue des Martyrs F-38054 Grenoble, France
3 Développement et Neuropharmacologie, CNRS UMR8542 Ecole Normale Supérieure 46 rue d’Ulm F-75005 Paris, France
*Author for correspondence (e-mail: joliot{at}biologie.ens.fr)
Accepted 30 April 2002
Chicken Engrailed 2 homeoprotein is transported between cells in culture. This intercellular transfer is based on unconventional secretion and internalisation mechanisms: Engrailed 2 has access to vesicles but lacks a signal sequence for secretion and is internalised by a non-endocytic process. We show that phosphorylation of a serine-rich domain within Engrailed 2 by the protein kinase CK2 specifically inhibits Engrailed 2 secretion. The availability of the serine-rich domain to CK2 is highly increased when it is displaced from its normal position to the C terminus of Engrailed 2, leading to a constitutive blockage of Engrailed 2 intercellular transfer. This indicates that intercellular transfer of Engrailed 2 is a highly regulated process.
Key words: Engrailed, Homeoprotein, Unconventional secretion, Phosphorylation, Regulation
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