Please use this identifier to cite or link to this item: https://doi.org/10.1080/09687680410001716871
Title: Mutually exclusive interactions of EHD1 with GS32 and syndapin II
Authors: Xut, Y.
Shit, H.
Wei, S.
Wong, S.H.
Hong, W. 
Keywords: EH domain
EHD1
Endocytosis
GS32
NPF motif
Syndapin II
Issue Date: Jul-2004
Citation: Xut, Y., Shit, H., Wei, S., Wong, S.H., Hong, W. (2004-07). Mutually exclusive interactions of EHD1 with GS32 and syndapin II. Molecular Membrane Biology 21 (4) : 269-277. ScholarBank@NUS Repository. https://doi.org/10.1080/09687680410001716871
Abstract: GS32/SNAP-29 is a SNAP-25-like SNARE and has been shown to interact with syntaxin 6. Using immobilized recombinant GS32, we have recovered EHD1 as a major GS32-interacting protein from total HeLa cell extracts. This interaction is mediated by the EH domain of EHD1 and the N-terminal NPF-containing 17-residue region of GS32. Co-immunoprecipitation suggests that GS32 could also interact with EHD1 in intact cells. When immobilized GST-EHD1 was used to fish out interacting proteins from total brain extracts, syndapin II was identified as a major interacting partner. Similar to the GS32-EHD1 interaction, syndapin II also interacts with the EH domain of EHD1 via its NPF repeat region. Interaction of endogenous EHD1 and syndapin II was also established by co-immunoprecipitation. Furthermore, interaction of GS32 and syndapin II with EHD1 was shown to be mutually exclusive, suggesting that EHD1 may regulate/participate in the functional pathways of both GS32 and syndapin II in a mutual exclusive manner. Opposing roles of GS32 and syndapin II in regulating the surface level of transferrin receptor (TfR) were observed.
Source Title: Molecular Membrane Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/113560
ISSN: 09687688
DOI: 10.1080/09687680410001716871
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