Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15.

TY - JOUR

T1 - Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15.

AU - Haffner, C

AU - Takei, K

AU - Chen, H

AU - Ringstad, N

AU - Hudson, A

AU - Butler, M H

AU - Salcini, A E

AU - Di Fiore, P P

AU - De Camilli, P

N1 - Keywords: Amino Acid Sequence; Animals; Calcium-Binding Proteins; Clathrin; Endocytosis; Humans; Immunohistochemistry; Intracellular Signaling Peptides and Proteins; Molecular Sequence Data; Nerve Endings; Nerve Tissue Proteins; Phosphoproteins; Phosphoric Monoester Hydrolases; Rats; Sequence Alignment; Synaptic Transmission; Synaptic Vesicles

PY - 1997

Y1 - 1997

N2 - Synaptojanin 1 is an inositol 5-phosphatase with a putative role in clathrin-mediated endocytosis. Goal of this study was to provide new evidence for this hypothesis. We show that synaptojanin 1 is concentrated at clathrin-coated endocytic intermediates in nerve terminals. Furthermore, we report that synaptojanin-170, an alternatively spliced isoform of synaptojanin 1, binds Eps15, a clathrin coat-associated protein. Binding is mediated by the COOH-terminal region of synaptojanin-170 which we show here to be poorly conserved from rat to humans, but to contain in both species three asparagine-proline-phenylalanine (NPF) repeats. This motif has been found to be the core of the binding site for the EH domains of Eps15. Together with previous data, our results suggest that synaptojanin 1 can be recruited to clathrin-coated pits via a multiplicity of interactions.

AB - Synaptojanin 1 is an inositol 5-phosphatase with a putative role in clathrin-mediated endocytosis. Goal of this study was to provide new evidence for this hypothesis. We show that synaptojanin 1 is concentrated at clathrin-coated endocytic intermediates in nerve terminals. Furthermore, we report that synaptojanin-170, an alternatively spliced isoform of synaptojanin 1, binds Eps15, a clathrin coat-associated protein. Binding is mediated by the COOH-terminal region of synaptojanin-170 which we show here to be poorly conserved from rat to humans, but to contain in both species three asparagine-proline-phenylalanine (NPF) repeats. This motif has been found to be the core of the binding site for the EH domains of Eps15. Together with previous data, our results suggest that synaptojanin 1 can be recruited to clathrin-coated pits via a multiplicity of interactions.

M3 - Journal article

C2 - 9428629

SN - 0014-5793

VL - 419

SP - 175

EP - 180

JO - F E B S Letters

JF - F E B S Letters

IS - 2-3

ER -