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    FEBS Lett. 2002 Jan 30;511(1-3):155-8.

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

    Jacobsen L, Madsen P, Nielsen MS, Geraerts WP, Gliemann J, Smit AB, Petersen CM.

    Source

    Department of Molecular and Cellular Neurobiology, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands. lija@bio.vu.nl

    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 (psi-psi-X-X-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains.

    PMID:
    11821067
    [PubMed - indexed for MEDLINE]

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