The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.
We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and -2, which take part in Golgi-endosome sorting. The GGAs bind with differential requirements via three critical residues in the C-terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6-phosphate receptors, the GGA-binding ... segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (psi-psi-X-X-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains.
Mesh Terms:
ADP-Ribosylation Factors, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Binding Sites, Carrier Proteins, Cytoplasm, Golgi Apparatus, Hydrophobicity, Methionine, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Proteins, Receptors, LDL, Two-Hybrid System Techniques
ADP-Ribosylation Factors, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Binding Sites, Carrier Proteins, Cytoplasm, Golgi Apparatus, Hydrophobicity, Methionine, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Proteins, Receptors, LDL, Two-Hybrid System Techniques
FEBS Lett.
Date: Jan. 30, 2002
PubMed ID: 11821067
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