1lf8
Complex of GGA3-VHS Domain and CI-MPR C-terminal PhosphopeptideComplex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide
Structural highlights
FunctionGGA3_HUMAN Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPhosphorylation 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. Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism.,Kato Y, Misra S, Puertollano R, Hurley JH, Bonifacino JS Nat Struct Biol. 2002 Jul;9(7):532-6. PMID:12032548[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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