Calsenilin and calp interact with the cytoplasmic tail of UDP-GAL:GA2/GM2/GD2 _-1,3-galactosyltransferase

QUINTERO C; VALDEZ TAUBAS J; FERRARI M; HAEDO S; MACCIONI HJF

PORTLAND PRESS LTD

Año: 2008 vol. 15 p. 19 - 19

ynopsis UDP-Gal: GA2/GM2/GD2 £]-1,3 galactosyltransferase (GalT2) is a Golgi resident, type II membrane protein, that participates in the synthesis of glycosphingolipids. molecular determinants for traffic and localization of this and other glycosyltransferases are still poorly characterized. Considering the possibility interactions with other proteins may influence these processes, we carried out a yeast two-hybrid screening using elements of the N-terminal domain of GalT2 as bait. this screening, we identified Calsenilin and its close homologue CALP (Calsenilinlike protein), both members of the Recoverin-Neuronal Calcium Sensor (NCS) family of calcium binding proteins. In vitro, GalT2 binds to immobilized recombinant CALP, and CALP binds to immobilized peptides with the GalT2 cytoplasmic sequence. GalT2 and Calsenilin interact physically when co-expressed in CHO- cells. The expression of CALP or Calsenilin affect Golgi localization of GalT2, and other two glycosyltransf