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.
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
J. Cell. Sci.
Date: Dec. 01, 2000
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