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- Title
Transmembrane transforming growth factor-a tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55.
- Authors
Kuo, Alfred; Zhong, Cuiling; Lane, William S.; Derynck, Rik
- Abstract
Transforming growth factor-α (TGF-α) and related proteins represent a family of transmembrane growth factors with representatives in flies and worms. Little is known about the transport of TGF-α and other transmembrane growth factors to the cell surface and its regulation. p59 was purified as a cytoplasmic protein, which at endogenous levels associates with transmembrane TGF-α. eDNA cloning of p59 revealed a 452 amino acid sequence with two PDZ domains. p59 is myristoylated and palmitoylated, and associates with the Golgi system, where it co-localizes with TGF-α. Its first PDZ domain interacts with the C-terminus of transmembrane TGF-α and select transmembrane proteins. p59 is the human homolog of GRASP55, which is structurally related to GRASP65. GRASP55 and GRASP65 have been shown to play a role in stacking of the Golgi cisternae in vitro. C-terminal mutations of transmembrane TGF-α, which decrease or abolish the interaction with p59, also strongly impair cell surface expression of TGF-α. Our observations suggest a role for membrane tethering of p59/GRASP55 to select transmembrane proteins, including TGF-α, in maturation and transport to the cell surface.
- Subjects
GROWTH factors; PROTEINS; WORMS; CYTOPLASM; AMINO acids; CELLS; GENETIC mutation
- Publication
EMBO Journal, 2000, Vol 19, Issue 23, p6427
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/19.23.6427