1LF8

Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide

Summary for 1LF8

• Entry DOI: 10.2210/pdb1lf8/pdb
• Related: 1JPL 1JUQ 1JWF 1JWG
• Descriptor: ADP-ribosylation factor binding protein GGA3, Cation-independent mannose-6-phosphate receptor (3 entities in total)
• Functional Keywords: vhs domain, protein-phosphopeptide complex, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9NZ52; Lysosome membrane; Single-pass type I membrane protein: P11717
• Total number of polymer chains: 8
• Total formula weight: 84079.72

Authors

Kato, Y.,Misra, S.,Puertollano, R.,Hurley, J.H.,Bonifacino, J.S. (deposition date: 2002-04-10, release date: 2002-06-26, Last modification date: 2024-10-30)

Primary citation

Kato, Y.,Misra, S.,Puertollano, R.,Hurley, J.H.,Bonifacino, J.S.
Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism.
Nat.Struct.Biol., 9:532-536, 2002

PubMed Abstract: Phosphorylation of the cytosolic tails of transmembrane receptors can regulate their intracellular trafficking. The structural basis for such regulation, however, has not been explained in most cases. The cytosolic tail of the cation-independent mannose 6-phosphate receptor contains a serine residue within an acidic-cluster dileucine signal that is important for the function of the receptor in the biosynthetic sorting of lysosomal hydrolases. We show here that phosphorylation of this Ser enhances interactions of the signal with its recognition module, the VHS domain of the GGA proteins. Crystallographic analyses demonstrate that the phosphoserine residue interacts electrostatically with two basic residues on the VHS domain of GGA3, thus providing an additional point of attachment of the acidic-cluster dileucine signal to its recognition module.

PubMed: 12032548

Experimental method

X-RAY DIFFRACTION (2.3 Å)