The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | FEBS Letters |
Volume | 511 |
Issue number | 1-3 |
Pages (from-to) | 155-8 |
Number of pages | 3 |
ISSN | 0014-5793 |
Publication status | Published - 2002 |
Externally published | Yes |
Bibliographical note
Keywords: 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
ID: 5034402