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All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis.

The PACSINs are a family of cytoplasmic phosphoproteins that play a role in vesicle formation and transport. We report the cloning and cDNA sequencing of PACSIN 3 and the analysis of all three PACSIN isoforms with regard to tissue distribution, ligand binding properties and influence on endocytosis. PACSIN 3 differs from the other family members in having a short proline-rich region and lacking asparagine-proline-phenylalanine motifs. In contrast to the neurospecific PACSIN 1 and the ubiquitously expressed PACSIN 2, PACSIN 3 is mainly detected in lung and muscle tissues. All isoforms potentially oligomerize and bind to dynamin, synaptojanin 1 and N-WASP via their Src homology 3 domains. The PACSIN proteins colocalize with dynamin, but not with clathrin, implying a specific role with a distinct subpopulation of dynamin at defined cellular sites. Transferrin endocytosis is blocked in a dose-dependent manner in cells overexpressing the PACSIN variants, but the inhibitory effect can be abolished by mutating specific amino acid residues in the Src homology 3 domains. These characteristics of the PACSIN protein family suggest a general function in recruitment of the interacting proteins to sites of endocytosis.

Pubmed ID: 11082044

Authors

  • Modregger J
  • Ritter B
  • Witter B
  • Paulsson M
  • Plomann M

Journal

Journal of cell science

Publication Data

December 29, 2000

Associated Grants

None

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA, Complementary
  • Dynamins
  • Endocytosis
  • GTP Phosphohydrolases
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mice
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Phosphoproteins
  • Phosphoric Monoester Hydrolases
  • Protein Isoforms
  • Proteins
  • Tissue Distribution
  • Transferrin
  • Wiskott-Aldrich Syndrome Protein, Neuronal