A functional PtdIns(3)P-binding motif View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-07

AUTHORS

Varsha Patki, Deirdre C. Lawe, Silvia Corvera, Joseph V. Virbasius, Anil Chawla

ABSTRACT

Treating cells with the phosphatidylinositol-3-OH kinase (PI(3)K) inhibitor wortmannin causes the dissociation of the early-endosomal antigen EEA1 from early endosomes1. EEA1 from cytosolic extracts binds to liposomes containing phosphatidylinositol-3-phosphate (PtdIns(3)P), the major product of PI(3)K in yeast and mammalian cells1,2. Here we show that a RING zinc-finger domain at the carboxy terminus of EEA1, previously identified and named the ‘FYVE’ domain3, binds directly and specifically to PtdIns(3)P. This indicates that proteins containing this motif may be downstream effectors of PI(3)K in yeast and mammalian cells. More... »

PAGES

433-434

References to SciGraph publications

  • 1998-07. FYVE fingers bind PtdIns(3)P in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/28771

    DOI

    http://dx.doi.org/10.1038/28771

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1001927676

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9697765


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