Crn7 interacts with AP-1 and is required for the maintenance of Golgi morphology and protein export from the Golgi

Vasily Rybakin*, Natalia V. Gounko, Kira Späte, Stefan Höning, Irina V. Majoul, Rainer Duden, Angelika A. Noegel

*Corresponding author for this work
25 Citations (Scopus)

Abstract

Crn7 is a novel cytosolic mammalian WD-repeat protein of unknown function that associates with Golgi membranes. Here, we demonstrate that Crn7 knockdown by small interfering RNA results in dramatic changes in the Golgi morphology and function. First, the Golgi ribbon is disorganized in Crn7 KD cells. Second, the Golgi export of several marker proteins including VSV envelope G glycoprotein is greatly reduced but not the retrograde protein import into the Golgi complex. We further establish that Crn7 co-precipitates with clathrin adaptor AP-1 but is not required for AP-1 targeting to Golgi membranes. We identify tyrosine 288-based motif as part of a canonical YXXΦ sorting signal and a major μ1-adaptin binding site in vitro. This study provides the first insight into the function of mammalian Crn7 protein in the Golgi complex.

Original languageEnglish
JournalJournal of Biological Chemistry
Volume281
Issue number41
Pages (from-to)31070-31078
Number of pages9
ISSN0021-9258
DOIs
Publication statusPublished - 13.10.2006

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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