SCAMP1 function in endocytosis

J Biol Chem. 2000 Apr 28;275(17):12752-6. doi: 10.1074/jbc.275.17.12752.


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 gamma-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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Protein Complex 1
  • Adaptor Proteins, Vesicular Transport*
  • Animals
  • Brain / metabolism
  • COS Cells
  • Carrier Proteins / metabolism
  • Carrier Proteins / physiology*
  • Chromatography, Affinity
  • DNA, Complementary / metabolism
  • Endocytosis*
  • Gene Library
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins / physiology*
  • Molecular Sequence Data
  • Rats
  • Transfection
  • Transferrin / metabolism
  • Two-Hybrid System Techniques


  • Adaptor Protein Complex 1
  • Adaptor Proteins, Vesicular Transport
  • Carrier Proteins
  • DNA, Complementary
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Scamp1 protein, rat
  • Synrg protein, rat
  • Transferrin
  • intersectin 1

Associated data

  • GENBANK/AF242544