RGD Reference Report - Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15. - Rat Genome Database

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

Authors: Haffner, C  Takei, K  Chen, H  Ringstad, N  Hudson, A  Butler, MH  Salcini, AE  Di Fiore, PP  De Camilli, P 
Citation: Haffner C, etal., FEBS Lett. 1997 Dec 15;419(2-3):175-80.
RGD ID: 11059574
Pubmed: PMID:9428629   (View Abstract at PubMed)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Synj1Ratclathrin coat of coated pit part_ofIDA PMID:9428629ParkinsonsUK-UCL 
Synj1Ratmicrotubule located_inIDA PMID:9428629ParkinsonsUK-UCL 
Synj1Ratsynaptic membrane located_inIDA PMID:9428629ParkinsonsUK-UCL 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Synj1RatEH domain binding  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Synj1  (synaptojanin 1)


Additional Information