SCAMP1 function in endocytosis

Rafael Fernández-Chacón, Mircea Achiriloaie, Roger Janz, Joseph P. Albanesi, Thomas C. Südhof

Research output: Contribution to journalArticle

71 Scopus citations

Abstract

Secretory carrier membrane proteins (SCAMPs) are ubiquitous components of recycling vesicles that shuttle between the plasma membrane, endosomes, and the trans-Golgi complex. SCAMPs contain multiple N-terminal NPF repeats and four highly conserved transmembrane regions. NPF repeats often interact with EH domain proteins that function in budding of transport vesicles from the plasma membrane or the Golgi complex. We now show that the NPF repeats of SCAMP1 bind to two EH domain proteins, intersectin 1, which is involved in endocytic budding at the plasma membrane, and γ-synergin, which may mediate the budding of vesicles in the trans-Golgi complex. Expression of SCAMP1 lacking the N-terminal NPF repeats potently inhibited transferrin uptake by endocytosis. Our data suggest that one of the functions of SCAMPs is to participate in endocytosis via a mechanism which may involve the recruitment of clathrin coats to the plasma membrane and the trans-Golgi network.

Original languageEnglish (US)
Pages (from-to)12752-12756
Number of pages5
JournalJournal of Biological Chemistry
Volume275
Issue number17
DOIs
StatePublished - Apr 28 2000

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Fernández-Chacón, R., Achiriloaie, M., Janz, R., Albanesi, J. P., & Südhof, T. C. (2000). SCAMP1 function in endocytosis. Journal of Biological Chemistry, 275(17), 12752-12756. https://doi.org/10.1074/jbc.275.17.12752