The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding

L. Jacobsen, P. Madsen, M.S. Nielsen, W.P.M. Geraerts, J. Gliemann, A.B. Smit, C.M. Petersen

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

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 (Ψ-Ψ-X-X-∅) defining minimum requirements for GGA binding to cytoplasmic receptor domains. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Original languageEnglish
Pages (from-to)155-158
Number of pages4
JournalFEBS Letters
Volume511
Issue number1-3
DOIs
Publication statusPublished - 2002

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